9BVR
Vitamin K-dependent gamma-carboxylase with factor IX propeptide and partially carboxylated glutamate-rich region and with vitamin K hydroquinone and calcium
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005788 | cellular_component | endoplasmic reticulum lumen |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0007596 | biological_process | blood coagulation |
| A | 0008488 | molecular_function | gamma-glutamyl carboxylase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019842 | molecular_function | vitamin binding |
| A | 0036211 | biological_process | protein modification process |
| A | 0042373 | biological_process | vitamin K metabolic process |
| A | 0046929 | biological_process | negative regulation of neurotransmitter secretion |
| A | 0051604 | biological_process | protein maturation |
| A | 1903011 | biological_process | negative regulation of bone development |
| A | 2000225 | biological_process | negative regulation of testosterone biosynthetic process |
Functional Information from PROSITE/UniProt
| site_id | PS00011 |
| Number of Residues | 26 |
| Details | GLA_1 Vitamin K-dependent carboxylation domain. EcmEEkCsfeearEvfentertte.FW |
| Chain | Residue | Details |
| P | GLU63-TRP88 |
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 | 1 |
| 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 | 17 |
| Details | Propeptide: {"featureId":"PRO_0000027755","evidences":[{"source":"PubMed","id":"2592373","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14722079","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NL0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 5 |
| Details | Binding site: {"description":"via 4-carboxyglutamate","evidences":[{"source":"PubMed","id":"14722079","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1NL0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"via 4-carboxyglutamate","evidences":[{"source":"UniProtKB","id":"P00741","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"4-carboxyglutamate","evidences":[{"source":"UniProtKB","id":"P00741","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00463","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (GalNAc...) threonine","evidences":[{"source":"PubMed","id":"25456591","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
