LOCUS 1FEN_A 183 aa linear MAM 07-FEB-2024
DEFINITION Chain A, RETINOL BINDING PROTEIN.
ACCESSION 1FEN_A
VERSION 1FEN_A
DBSOURCE pdb: molecule 1FEN, chain A, release Feb 7, 2024;
deposition: Aug 29, 1994;
class: TRANSPORT PROTEIN;
source: Mmdb_id: 56119, Pdb_id 1: 1FEN;
Exp. method: X-ray Diffraction.
KEYWORDS .
SOURCE Bos taurus (domestic cattle)
ORGANISM Bos taurus
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
REFERENCE 1 (residues 1 to 183)
AUTHORS Zanotti,G., Ottonello,S., Berni,R. and Monaco,H.L.
TITLE Crystal structure of the trigonal form of human plasma
retinol-binding protein at 2.5 A resolution
JOURNAL J Mol Biol 230 (2), 613-624 (1993)
PUBMED 8464067
REFERENCE 2 (residues 1 to 183)
AUTHORS Zanotti,G., Berni,R. and Monaco,H.L.
TITLE Crystal structure of liganded and unliganded forms of bovine plasma
retinol-binding protein
JOURNAL J Biol Chem 268 (15), 10728-10738 (1993)
PUBMED 8496140
REFERENCE 3 (residues 1 to 183)
AUTHORS Zanotti,G., Malpeli,G. and Berni,R.
TITLE The interaction of N-ethyl retinamide with plasma retinol-binding
protein (RBP) and the crystal structure of the retinoid-RBP complex
at 1.9-A resolution
JOURNAL J Biol Chem 268 (33), 24873-24879 (1993)
PUBMED 8227049
REFERENCE 4 (residues 1 to 183)
AUTHORS Zanotti,G., Marcello,M., Malpeli,G., Folli,C., Sartori,G. and
Berni,R.
TITLE Crystallographic studies on complexes between retinoids and plasma
retinol-binding protein
JOURNAL J Biol Chem 269 (47), 29613-29620 (1994)
PUBMED 7961949
REFERENCE 5 (residues 1 to 183)
AUTHORS Zanotti,G., Marcello,M., Malpeli,G., Sartori,G. and Berni,R.
TITLE Direct Submission
JOURNAL Submitted (29-AUG-1994)
COMMENT CRYSTALLOGRAPHIC STUDIES ON COMPLEXES BETWEEN RETINOIDS AND PLASMA
RETINOL-BINDING PROTEIN.
FEATURES Location/Qualifiers
source 1..183
/organism="Bos taurus"
/db_xref="taxon:9913"
Region 4..174
/region_name="lipocalin_RBP_like"
/note="retinol-binding protein 4 and similar proteins;
cd00743"
/db_xref="CDD:381184"
Site order(20,24,29,32,35..37,43,45,53,55..57,61,63,73..75,77,
86,88,90,96..98,102,104,106,115,117,119,121,133,135,137)
/site_type="other"
/note="ligand binding cavity [chemical binding]"
/db_xref="CDD:381184"
SecStr 21..26
/sec_str_type="sheet"
/note="strand 1"
SecStr 27..32
/sec_str_type="sheet"
/note="strand 2"
Site order(29,32,35..37,43,45,55..57,61,63,73..75,77,88,90,
96..98,102,104,117,121,133,135,137)
/site_type="other"
/note="retinol binding site [chemical binding]"
/db_xref="CDD:381184"
SecStr 40..49
/sec_str_type="sheet"
/note="strand 3"
SecStr 51..58
/sec_str_type="sheet"
/note="strand 4"
SecStr 59..64
/sec_str_type="sheet"
/note="strand 5"
Site order(63..67,89,91,95..99)
/site_type="other"
/note="transthyretin interface [polypeptide binding]"
/db_xref="CDD:381184"
SecStr 66..71
/sec_str_type="sheet"
/note="strand 6"
SecStr 72..80
/sec_str_type="sheet"
/note="strand 7"
SecStr 84..89
/sec_str_type="sheet"
/note="strand 8"
SecStr 90..93
/sec_str_type="sheet"
/note="strand 9"
SecStr 99..103
/sec_str_type="sheet"
/note="strand 10"
SecStr 104..108
/sec_str_type="sheet"
/note="strand 11"
SecStr 113..122
/sec_str_type="sheet"
/note="strand 12"
SecStr 130..139
/sec_str_type="sheet"
/note="strand 13"
SecStr 146..159
/sec_str_type="helix"
/note="helix 1"
SecStr 165..168
/sec_str_type="sheet"
/note="strand 14"
ORIGIN
1 erdcrvssfr vkenfdkarf agtwyamakk dpeglflqdn ivaefsvden ghmsatakgr
61 vrllnnwdvc admvgtftdt edpakfkmky wgvasflqkg nddhwiidtd yetfavqysc
121 rllnldgtca dsysfvfard psgfspevqk ivrqrqeelc larqyrliph ngycdgkser
181 nil
//