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1D2B

THE MMP-INHIBITORY, N-TERMINAL DOMAIN OF HUMAN TISSUE INHIBITOR OF METALLOPROTEINASES-1 (N-TIMP-1), SOLUTION NMR, 29 STRUCTURES

Functional Information from GO Data
ChainGOidnamespacecontents
A0008191molecular_functionmetalloendopeptidase inhibitor activity
Functional Information from PROSITE/UniProt
site_idPS00288
Number of Residues13
DetailsTIMP Tissue inhibitors of metalloproteinases signature. CtCvPpHPQtaFC
ChainResidueDetails
ACYS1-CYS13

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:22427646
ChainResidueDetails
ACYS1

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Involved in metalloproteinase-binding => ECO:0000269|PubMed:22427646, ECO:0007744|PDB:3V96
ChainResidueDetails
ALEU34

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490
ChainResidueDetails
AASN30

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002
ChainResidueDetails
AASN78

237735

PDB entries from 2025-06-18

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