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3FBY

The crystal structure of the signature domain of cartilage oligomeric matrix protein.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0007155biological_processcell adhesion
B0005509molecular_functioncalcium ion binding
B0005576cellular_componentextracellular region
B0007155biological_processcell adhesion
C0005509molecular_functioncalcium ion binding
C0005576cellular_componentextracellular region
C0007155biological_processcell adhesion
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DFDADKVVDkiDV
ChainResidueDetails
AASP507-VAL519

site_idPS01186
Number of Residues14
DetailsEGF_2 EGF-like domain signature 2. CvCavGWagngil..C
ChainResidueDetails
ACYS253-CYS266

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues126
DetailsDomain: {"description":"EGF-like 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues96
DetailsRepeat: {"description":"TSP type-3 1"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues105
DetailsRepeat: {"description":"TSP type-3 2"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues66
DetailsRepeat: {"description":"TSP type-3 3"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues105
DetailsRepeat: {"description":"TSP type-3 4"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues66
DetailsRepeat: {"description":"TSP type-3 5"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues111
DetailsRepeat: {"description":"TSP type-3 6"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues105
DetailsRepeat: {"description":"TSP type-3 7"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues105
DetailsRepeat: {"description":"TSP type-3 8"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues642
DetailsDomain: {"description":"TSP C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00635","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues615
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues690
DetailsRegion: {"description":"Mediates cell survival and induction of the IAP family of survival proteins"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues6
DetailsMotif: {"description":"Cell attachment site","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues90
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues27
DetailsCompositional bias: {"description":"Acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19276170","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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