eF-site ID 6n9d-AB PDB Code 6n9d Chain A, B click to enlarge Title Complex of tissue inhibitor of metalloproteinases-1 (TIMP-1) mutant (L34G/L133P/L151C/G154A) with matrix metalloproteinase-3 catalytic domain (MMP-3cd) Classification HYDROLASE/HYDROLASE inhibitor Compound Stromelysin-1 Source (TIMP1_HUMAN) Sequence A:  PGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEE VTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAH AYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHEIGHS LGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLY G B:  CTCVPPHPQTAFCNSDLVIRAKFVGTPEVNQTTGYQRYEI KMTKMYKGFQALDIRFVYTPAMESVCGYFHRSHNRSEEFL IAGKLQDGLLHITTCSFVAPWNSLSLAQRRGFTKTYTVGC EECTVFPCPSIPCKLQSGTHCLWTDQCLQASEKGFQSRHL ACLPREPGLCTWQSL Description Functional site 1) chain A residue 158 type sequence D description binding site for residue CA A 301 source : AC1 2) chain A residue 159 type sequence G description binding site for residue CA A 301 source : AC1 3) chain A residue 161 type sequence G description binding site for residue CA A 301 source : AC1 4) chain A residue 163 type sequence V description binding site for residue CA A 301 source : AC1 5) chain A residue 181 type sequence D description binding site for residue CA A 301 source : AC1 6) chain A residue 184 type sequence E description binding site for residue CA A 301 source : AC1 7) chain A residue 105 type sequence T description binding site for residue CA A 302 source : AC2 8) chain A residue 107 type sequence D description binding site for residue CA A 302 source : AC2 9) chain A residue 182 type sequence D description binding site for residue CA A 302 source : AC2 10) chain A residue 184 type sequence E description binding site for residue CA A 302 source : AC2 11) chain A residue 151 type sequence H description binding site for residue ZN A 303 source : AC3 12) chain A residue 153 type sequence D description binding site for residue ZN A 303 source : AC3 13) chain A residue 166 type sequence H description binding site for residue ZN A 303 source : AC3 14) chain A residue 179 type sequence H description binding site for residue ZN A 303 source : AC3 15) chain A residue 201 type sequence H description binding site for residue ZN A 304 source : AC4 16) chain A residue 205 type sequence H description binding site for residue ZN A 304 source : AC4 17) chain A residue 211 type sequence H description binding site for residue ZN A 304 source : AC4 18) chain B residue 1 type sequence C description binding site for residue ZN A 304 source : AC4 19) chain A residue 140 type sequence A description binding site for residue CA A 305 source : AC5 20) chain A residue 141 type sequence D description binding site for residue CA A 305 source : AC5 21) chain A residue 173 type sequence G description binding site for residue CA A 305 source : AC5 22) chain A residue 175 type sequence N description binding site for residue CA A 305 source : AC5 23) chain A residue 177 type sequence D description binding site for residue CA A 305 source : AC5 24) chain A residue 198-207 type prosite sequence VAAHEIGHSL description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEIGHSL source prosite : PS00142 25) chain B residue 1-13 type prosite sequence CTCVPPHPQTAFC description TIMP Tissue inhibitors of metalloproteinases signature. CtCvPpHPQtaFC source prosite : PS00288 26) chain A residue 201 type catalytic sequence H description 591 source MCSA : MCSA1 27) chain A residue 202 type catalytic sequence E description 591 source MCSA : MCSA1 28) chain A residue 205 type catalytic sequence H description 591 source MCSA : MCSA1 29) chain A residue 211 type catalytic sequence H description 591 source MCSA : MCSA1 30) chain B residue 1 type BINDING sequence C description BINDING => ECO:0000269|PubMed:22427646 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 173 type SITE sequence G description Involved in metalloproteinase-binding => ECO:0000269|PubMed:22427646, ECO:0007744|PDB:3V96 source Swiss-Prot : SWS_FT_FI2 32) chain A residue 175 type SITE sequence N description Involved in metalloproteinase-binding => ECO:0000269|PubMed:22427646, ECO:0007744|PDB:3V96 source Swiss-Prot : SWS_FT_FI2 33) chain A residue 177 type SITE sequence D description Involved in metalloproteinase-binding => ECO:0000269|PubMed:22427646, ECO:0007744|PDB:3V96 source Swiss-Prot : SWS_FT_FI2 34) chain A residue 179 type SITE sequence H description Involved in metalloproteinase-binding => ECO:0000269|PubMed:22427646, ECO:0007744|PDB:3V96 source Swiss-Prot : SWS_FT_FI2 35) chain A residue 181 type SITE sequence D description Involved in metalloproteinase-binding => ECO:0000269|PubMed:22427646, ECO:0007744|PDB:3V96 source Swiss-Prot : SWS_FT_FI2 36) chain A residue 182 type SITE sequence D description Involved in metalloproteinase-binding => ECO:0000269|PubMed:22427646, ECO:0007744|PDB:3V96 source Swiss-Prot : SWS_FT_FI2 37) chain A residue 184 type SITE sequence E description Involved in metalloproteinase-binding => ECO:0000269|PubMed:22427646, ECO:0007744|PDB:3V96 source Swiss-Prot : SWS_FT_FI2 38) chain A residue 151 type SITE sequence H description Involved in metalloproteinase-binding => ECO:0000269|PubMed:22427646, ECO:0007744|PDB:3V96 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 153 type SITE sequence D description Involved in metalloproteinase-binding => ECO:0000269|PubMed:22427646, ECO:0007744|PDB:3V96 source Swiss-Prot : SWS_FT_FI2 40) chain A residue 158 type SITE sequence D description Involved in metalloproteinase-binding => ECO:0000269|PubMed:22427646, ECO:0007744|PDB:3V96 source Swiss-Prot : SWS_FT_FI2 41) chain A residue 159 type SITE sequence G description Involved in metalloproteinase-binding => ECO:0000269|PubMed:22427646, ECO:0007744|PDB:3V96 source Swiss-Prot : SWS_FT_FI2 42) chain A residue 161 type SITE sequence G description Involved in metalloproteinase-binding => ECO:0000269|PubMed:22427646, ECO:0007744|PDB:3V96 source Swiss-Prot : SWS_FT_FI2 43) chain A residue 163 type SITE sequence V description Involved in metalloproteinase-binding => ECO:0000269|PubMed:22427646, ECO:0007744|PDB:3V96 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 166 type SITE sequence H description Involved in metalloproteinase-binding => ECO:0000269|PubMed:22427646, ECO:0007744|PDB:3V96 source Swiss-Prot : SWS_FT_FI2 45) chain B residue 34 type SITE sequence G description Involved in metalloproteinase-binding => ECO:0000269|PubMed:22427646, ECO:0007744|PDB:3V96 source Swiss-Prot : SWS_FT_FI2 46) chain B residue 135 type SITE sequence I description Involved in metalloproteinase-binding => ECO:0000269|PubMed:22427646, ECO:0007744|PDB:3V96 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 211 type MOD_RES sequence H description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI3 48) chain A residue 205 type MOD_RES sequence H description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI3 49) chain B residue 155 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI3 50) chain B residue 30 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490 source Swiss-Prot : SWS_FT_FI4 51) chain B residue 78 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002 source Swiss-Prot : SWS_FT_FI5

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