9MQC
Vitamin K-dependent gamma-carboxylase with Osteocalcin (mutant) and vitamin K hydroquinone
This is a non-PDB format compatible entry.
Functional Information from PROSITE/UniProt
site_id | PS00011 |
Number of Residues | 26 |
Details | GLA_1 Vitamin K-dependent carboxylation domain. EprREvCelnpdcDeladhigfqe.AY |
Chain | Residue | Details |
P | GLU68-TYR93 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 100 |
Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 165 |
Details | Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 48 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17073445","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P02820","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Modified residue: {"description":"4-carboxyglutamate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00463","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"6967872","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |