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7UAI

Meprin alpha helix in complex with fetuin-B

Functional Information from GO Data
ChainGOidnamespacecontents
A0004869molecular_functioncysteine-type endopeptidase inhibitor activity
A0005615cellular_componentextracellular space
B0004222molecular_functionmetalloendopeptidase activity
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0016020cellular_componentmembrane
C0004222molecular_functionmetalloendopeptidase activity
C0006508biological_processproteolysis
C0008237molecular_functionmetallopeptidase activity
C0008270molecular_functionzinc ion binding
C0016020cellular_componentmembrane
D0004222molecular_functionmetalloendopeptidase activity
D0006508biological_processproteolysis
D0008237molecular_functionmetallopeptidase activity
D0008270molecular_functionzinc ion binding
D0016020cellular_componentmembrane
E0004222molecular_functionmetalloendopeptidase activity
E0006508biological_processproteolysis
E0008237molecular_functionmetallopeptidase activity
E0008270molecular_functionzinc ion binding
E0016020cellular_componentmembrane
H0004869molecular_functioncysteine-type endopeptidase inhibitor activity
H0005615cellular_componentextracellular space
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. IIEHEILHAL
ChainResidueDetails
EILE152-LEU161

site_idPS00740
Number of Residues41
DetailsMAM_1 MAM domain signature. GyFMqfsTssgsaeeaal.LesriLypkrkqqCLqFfYkmtG
ChainResidueDetails
EGLY312-GLY352

site_idPS01254
Number of Residues119
DetailsFETUIN_1 Fetuin family signature 1. CNDsdvlavagfalrdinkdrkdgyvlrlnrvndaqeyrrgglgslfyltldvletdCHvlrkkawqdCgmriffesvygq..CkaifymnnpsrvlylaaynCtlrpvskkkiymtCpdC
ChainResidueDetails
ACYS36-CYS154

site_idPS01255
Number of Residues10
DetailsFETUIN_2 Fetuin family signature 2. DvLETdCHvL
ChainResidueDetails
AASP87-LEU96

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues776
DetailsDomain: {"description":"Peptidase M12A","evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues507
DetailsDomain: {"description":"MAM","evidences":[{"source":"PROSITE-ProRule","id":"PRU00128","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues477
DetailsDomain: {"description":"MATH","evidences":[{"source":"PROSITE-ProRule","id":"PRU00129","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues29
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues19
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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