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4GWN

Crystal structure of human mature meprin beta

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TVQHEFLHAL
ChainResidueDetails
ATHR149-LEU158

site_idPS00740
Number of Residues41
DetailsMAM_1 MAM domain signature. GfFMhfdSssvnvgatav.LesrtLypkrgfqCLqFyLynsG
ChainResidueDetails
AGLY309-GLY349

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues194
DetailsDomain: {"description":"Peptidase M12A","evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues169
DetailsDomain: {"description":"MAM","evidences":[{"source":"PROSITE-ProRule","id":"PRU00128","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues155
DetailsDomain: {"description":"MATH","evidences":[{"source":"PROSITE-ProRule","id":"PRU00129","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22988105","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4GWM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Mediates preference for acidic residues at subsite P1'"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues7
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22988105","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GalNAc...) serine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GalNAc...) threonine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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