LOCUS 2EIC_A 639 aa linear PLN 31-OCT-2024
DEFINITION Chain A, Galactose oxidase.
ACCESSION 2EIC_A
VERSION 2EIC_A
DBSOURCE pdb: molecule 2EIC, chain A, release Oct 30, 2024;
deposition: Mar 12, 2007;
class: OXIDOREDUCTASE;
source: Mmdb_id: 45605, Pdb_id 1: 2EIC;
Exp. method: X-ray Diffraction.
KEYWORDS .
SOURCE Fusarium graminearum (Gibberella zeae)
ORGANISM Fusarium graminearum
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
Fusarium.
REFERENCE 1 (residues 1 to 639)
AUTHORS Rogers,M.S., Tyler,E.M., Akyumani,N., Kurtis,C.R., Spooner,R.K.,
Deacon,S.E., Tamber,S., Firbank,S.J., Mahmoud,K., Knowles,P.F.,
Phillips,S.E., McPherson,M.J. and Dooley,D.M.
TITLE The stacking tryptophan of galactose oxidase: a second-coordination
sphere residue that has profound effects on tyrosyl radical
behavior and enzyme catalysis
JOURNAL Biochemistry 46 (15), 4606-4618 (2007)
PUBMED 17385891
REFERENCE 2 (residues 1 to 639)
AUTHORS Akyumani,N., Tamber,S., Firbank,S.J., Knowles,P.F., Phillips,S.E.
and McPherson,M.J.
TITLE Direct Submission
JOURNAL Submitted (12-MAR-2007)
COMMENT Crystal Structure of Galactose Oxidase mutant W290F.
FEATURES Location/Qualifiers
source 1..639
/organism="Fusarium graminearum"
/db_xref="taxon:5518"
Region join(1..170,492..537)
/region_name="Domain 1"
/note="NCBI Domains"
Region 4..134
/region_name="FA58C"
/note="Coagulation factor 5/8 C-terminal domain, discoidin
domain; Cell surface-attached carbohydrate-binding domain,
present in eukaryotes and assumed to have horizontally
transferred to eubacterial genomes; cd00057"
/db_xref="CDD:238014"
SecStr 14..19
/sec_str_type="sheet"
/note="strand 1"
Bond bond(18,27)
/bond_type="disulfide"
Het join(bond(29),bond(32),bond(34),bond(37),bond(37),
bond(141),bond(142))
/heterogen="(NA,4827)"
SecStr 38..41
/sec_str_type="sheet"
/note="strand 2"
Site order(40,73,80)
/site_type="other"
/note="sugar binding site [chemical binding]"
/db_xref="CDD:238014"
SecStr 52..59
/sec_str_type="sheet"
/note="strand 3"
SecStr 62..65
/sec_str_type="sheet"
/note="strand 4"
SecStr 66..72
/sec_str_type="sheet"
/note="strand 5"
SecStr 83..91
/sec_str_type="sheet"
/note="strand 6"
SecStr 100..105
/sec_str_type="sheet"
/note="strand 7"
SecStr 111..116
/sec_str_type="sheet"
/note="strand 8"
SecStr 118..123
/sec_str_type="sheet"
/note="strand 9"
SecStr 124..130
/sec_str_type="sheet"
/note="strand 10"
SecStr 137..140
/sec_str_type="sheet"
/note="strand 11"
SecStr 141..148
/sec_str_type="sheet"
/note="strand 12"
Region <156..314
/region_name="NanM"
/note="N-acetylneuraminic acid mutarotase [Cell
wall/membrane/envelope biogenesis]; COG3055"
/db_xref="CDD:442289"
SecStr 158..162
/sec_str_type="sheet"
/note="strand 13"
SecStr 163..168
/sec_str_type="sheet"
/note="strand 14"
Region join(171..223,538..639)
/region_name="Domain 2"
/note="NCBI Domains"
SecStr 172..179
/sec_str_type="sheet"
/note="strand 15"
SecStr 180..189
/sec_str_type="sheet"
/note="strand 16"
SecStr 201..209
/sec_str_type="sheet"
/note="strand 17"
SecStr 211..220
/sec_str_type="sheet"
/note="strand 18"
Region 224..381
/region_name="Domain 3"
/note="NCBI Domains"
SecStr 227..235
/sec_str_type="sheet"
/note="strand 19"
Region 236..513
/region_name="NanM"
/note="N-acetylneuraminic acid mutarotase [Cell
wall/membrane/envelope biogenesis]; COG3055"
/db_xref="CDD:442289"
SecStr 237..245
/sec_str_type="sheet"
/note="strand 20"
SecStr 249..256
/sec_str_type="sheet"
/note="strand 21"
SecStr 257..263
/sec_str_type="sheet"
/note="strand 22"
Region 270..314
/region_name="KELCH repeat"
/note="KELCH repeat [structural motif]"
/db_xref="CDD:276965"
Het join(bond(272),bond(496),bond(581))
/heterogen="(CU1,4828)"
SecStr 275..279
/sec_str_type="sheet"
/note="strand 23"
SecStr 281..287
/sec_str_type="sheet"
/note="strand 24"
SecStr 298..305
/sec_str_type="sheet"
/note="strand 25"
SecStr 306..313
/sec_str_type="sheet"
/note="strand 26"
SecStr 335..341
/sec_str_type="sheet"
/note="strand 27"
SecStr 343..349
/sec_str_type="sheet"
/note="strand 28"
SecStr 352..360
/sec_str_type="sheet"
/note="strand 29"
SecStr 362..374
/sec_str_type="sheet"
/note="strand 30"
SecStr 375..378
/sec_str_type="sheet"
/note="strand 31"
Region 382..491
/region_name="Domain 4"
/note="NCBI Domains"
SecStr 384..392
/sec_str_type="sheet"
/note="strand 32"
SecStr 393..402
/sec_str_type="sheet"
/note="strand 33"
SecStr 407..412
/sec_str_type="sheet"
/note="strand 34"
SecStr 413..419
/sec_str_type="sheet"
/note="strand 35"
SecStr 426..431
/sec_str_type="sheet"
/note="strand 36"
SecStr 442..448
/sec_str_type="sheet"
/note="strand 37"
SecStr 450..456
/sec_str_type="sheet"
/note="strand 38"
SecStr 459..462
/sec_str_type="sheet"
/note="strand 39"
SecStr 472..478
/sec_str_type="sheet"
/note="strand 40"
SecStr 481..487
/sec_str_type="sheet"
/note="strand 41"
SecStr 495..503
/sec_str_type="sheet"
/note="strand 42"
SecStr 505..513
/sec_str_type="sheet"
/note="strand 43"
Bond bond(515,518)
/bond_type="disulfide"
SecStr 523..531
/sec_str_type="sheet"
/note="strand 44"
Region 538..637
/region_name="E_set_GO_C"
/note="C-terminal Early set domain associated with the
catalytic domain of galactose oxidase; cd02851"
/db_xref="CDD:199882"
SecStr 544..550
/sec_str_type="sheet"
/note="strand 45"
SecStr 552..556
/sec_str_type="sheet"
/note="strand 46"
SecStr 557..566
/sec_str_type="sheet"
/note="strand 47"
SecStr 569..580
/sec_str_type="sheet"
/note="strand 48"
SecStr 586..592
/sec_str_type="sheet"
/note="strand 49"
SecStr 594..597
/sec_str_type="sheet"
/note="strand 50"
SecStr 600..607
/sec_str_type="sheet"
/note="strand 51"
SecStr 615..624
/sec_str_type="sheet"
/note="strand 52"
SecStr 633..639
/sec_str_type="sheet"
/note="strand 53"
ORIGIN
1 asapigsais rnnwavtcds aqsgnecnka idgnkdtfwh tfygangdpk pphtytidmk
61 ttqnvnglsm lprqdgnqng wigrhevyls sdgtnwgspv asgswfadst tkysnfetrp
121 aryvrlvait eangqpwtsi aeinvfqass ytapqpglgr wgptidlpiv paaaaiepts
181 grvlmwssyr ndafggspgg itltsswdps tgivsdrtvt vtkhdmfcpg ismdgngqiv
241 vtggndakkt slydsssdsw ipgpdmqvar gyqssatmsd grvftiggsf sggvfeknge
301 vyspssktwt slpnakvnpm ltadkqglyr sdnhawlfgw kkgsvfqagp stamnwyyts
361 gsgdvksagk rqsnrgvapd amcgnavmyd avkgkiltfg gspdyqdsda ttnahiitlg
421 epgtspntvf asnglyfart fhtsvvlpdg stfitggqrr gipfedstpv ftpeiyvpeq
481 dtfykqnpns ivrvyhsisl llpdgrvfng ggglcgdctt nhfdaqiftp nylynsngnl
541 atrpkitrts tqsvkvggri tistdssisk aslirygtat htvntdqrri pltltnnggn
601 sysfqvpsds gvalpgywml fvmnsagvps vastirvtq
//