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6HT9

Mouse fetuin-B in complex with crayfish astacin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
B0004857molecular_functionenzyme inhibitor activity
B0004866molecular_functionendopeptidase inhibitor activity
B0004869molecular_functioncysteine-type endopeptidase inhibitor activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0007338biological_processsingle fertilization
B0007339biological_processbinding of sperm to zona pellucida
B0008191molecular_functionmetalloendopeptidase inhibitor activity
B0010951biological_processnegative regulation of endopeptidase activity
B0030414molecular_functionpeptidase inhibitor activity
B0060255biological_processregulation of macromolecule metabolic process
C0004222molecular_functionmetalloendopeptidase activity
C0006508biological_processproteolysis
C0008237molecular_functionmetallopeptidase activity
C0008270molecular_functionzinc ion binding
D0004857molecular_functionenzyme inhibitor activity
D0004866molecular_functionendopeptidase inhibitor activity
D0004869molecular_functioncysteine-type endopeptidase inhibitor activity
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0007338biological_processsingle fertilization
D0007339biological_processbinding of sperm to zona pellucida
D0008191molecular_functionmetalloendopeptidase inhibitor activity
D0010951biological_processnegative regulation of endopeptidase activity
D0030414molecular_functionpeptidase inhibitor activity
D0060255biological_processregulation of macromolecule metabolic process
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TIIHELMHAI
ChainResidueDetails
ATHR89-ILE98

site_idPS01254
Number of Residues119
DetailsFETUIN_1 Fetuin family signature 1. CNDsevlavagfalqninrdqkdgymlslnrvhdvrehyqedmgslfyltldvletdCHvlsrkaqkdCkprmfyesvygq..CkamfhinkprrvlylpaynCtlrpvskrkthttCpdC
ChainResidueDetails
BCYS39-CYS157

site_idPS01255
Number of Residues10
DetailsFETUIN_2 Fetuin family signature 2. DvLETdCHvL
ChainResidueDetails
BASP90-LEU99

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsPropeptide: {"featureId":"PRO_0000028874"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues396
DetailsDomain: {"description":"Peptidase M12A","evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1319561","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1319561","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8756323","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues42
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues28
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9UGM5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17330941","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues113
DetailsDomain: {"description":"Cystatin fetuin-B-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00862","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 403
ChainResidueDetails
AHIS92metal ligand
AGLU93proton shuttle (general acid/base)
AHIS96metal ligand
AHIS102metal ligand
ATYR149transition state stabiliser

site_idMCSA2
Number of Residues5
DetailsM-CSA 403
ChainResidueDetails
CHIS92metal ligand
CGLU93proton shuttle (general acid/base)
CHIS96metal ligand
CHIS102metal ligand
CTYR149transition state stabiliser

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PDB entries from 2025-07-30

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