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
Chain | GOid | namespace | contents |
A | 0008191 | molecular_function | metalloendopeptidase inhibitor activity |
Functional Information from PROSITE/UniProt
site_id | PS00288 |
Number of Residues | 13 |
Details | TIMP Tissue inhibitors of metalloproteinases signature. CtCvPpHPQtaFC |
Chain | Residue | Details |
A | CYS1-CYS13 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22427646 |
Chain | Residue | Details |
A | CYS1 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | SITE: Involved in metalloproteinase-binding => ECO:0000269|PubMed:22427646, ECO:0007744|PDB:3V96 |
Chain | Residue | Details |
A | LEU34 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490 |
Chain | Residue | Details |
A | ASN30 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002 |
Chain | Residue | Details |
A | ASN78 |