eF-site ID 2jt6-A PDB Code 2jt6 Chain A click to enlarge Title Solution structure of matrix metalloproteinase 3 (MMP-3) in the presence of 3-4'-cyanobyphenyl-4-yloxy)-n-hdydroxypropionamide (MMP-3 inhibitor VII) Classification HYDROLASE Compound Stromelysin-1 Source (MMP3_HUMAN) Sequence A:  GIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEV TPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHA YAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHEIGHSL GLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYG P Description (1)  Stromelysin-1 (E.C.3.4.24.17) Functional site 1) chain A residue 201 type sequence H description BINDING SITE FOR RESIDUE ZN A 256 source : AC1 2) chain A residue 205 type sequence H description BINDING SITE FOR RESIDUE ZN A 256 source : AC1 3) chain A residue 211 type sequence H description BINDING SITE FOR RESIDUE ZN A 256 source : AC1 4) chain A residue 151 type sequence H description BINDING SITE FOR RESIDUE ZN A 257 source : AC2 5) chain A residue 153 type sequence D description BINDING SITE FOR RESIDUE ZN A 257 source : AC2 6) chain A residue 166 type sequence H description BINDING SITE FOR RESIDUE ZN A 257 source : AC2 7) chain A residue 179 type sequence H description BINDING SITE FOR RESIDUE ZN A 257 source : AC2 8) chain A residue 158 type sequence D description BINDING SITE FOR RESIDUE CA A 258 source : AC3 9) chain A residue 159 type sequence G description BINDING SITE FOR RESIDUE CA A 258 source : AC3 10) chain A residue 161 type sequence G description BINDING SITE FOR RESIDUE CA A 258 source : AC3 11) chain A residue 163 type sequence V description BINDING SITE FOR RESIDUE CA A 258 source : AC3 12) chain A residue 181 type sequence D description BINDING SITE FOR RESIDUE CA A 258 source : AC3 13) chain A residue 184 type sequence E description BINDING SITE FOR RESIDUE CA A 258 source : AC3 14) chain A residue 139 type sequence E description BINDING SITE FOR RESIDUE CA A 259 source : AC4 15) chain A residue 141 type sequence D description BINDING SITE FOR RESIDUE CA A 259 source : AC4 16) chain A residue 173 type sequence G description BINDING SITE FOR RESIDUE CA A 259 source : AC4 17) chain A residue 175 type sequence N description BINDING SITE FOR RESIDUE CA A 259 source : AC4 18) chain A residue 177 type sequence D description BINDING SITE FOR RESIDUE CA A 259 source : AC4 19) chain A residue 165 type sequence A description BINDING SITE FOR RESIDUE JT6 A 1 source : AC5 20) chain A residue 201 type sequence H description BINDING SITE FOR RESIDUE JT6 A 1 source : AC5 21) chain A residue 202 type sequence E description BINDING SITE FOR RESIDUE JT6 A 1 source : AC5 22) chain A residue 205 type sequence H description BINDING SITE FOR RESIDUE JT6 A 1 source : AC5 23) chain A residue 211 type sequence H description BINDING SITE FOR RESIDUE JT6 A 1 source : AC5 24) chain A residue 216 type sequence E description BINDING SITE FOR RESIDUE JT6 A 1 source : AC5 25) chain A residue 217 type sequence A description BINDING SITE FOR RESIDUE JT6 A 1 source : AC5 26) chain A residue 220 type sequence Y description BINDING SITE FOR RESIDUE JT6 A 1 source : AC5 27) chain A residue 223 type sequence Y description BINDING SITE FOR RESIDUE JT6 A 1 source : AC5 28) chain A residue 201 type catalytic sequence H description 591 source MCSA : MCSA1 29) chain A residue 202 type catalytic sequence E description 591 source MCSA : MCSA1 30) chain A residue 205 type catalytic sequence H description 591 source MCSA : MCSA1 31) chain A residue 211 type catalytic sequence H description 591 source MCSA : MCSA1 32) chain A residue 198-207 type prosite sequence VAAHEIGHSL description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEIGHSL source prosite : PS00142 33) chain A residue 202 type ACT_SITE sequence E description source Swiss-Prot : SWS_FT_FI1 34) chain A residue 107 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 35) chain A residue 173 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 36) chain A residue 175 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 37) chain A residue 177 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 38) chain A residue 179 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 39) chain A residue 181 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 40) chain A residue 182 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 41) chain A residue 184 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 42) chain A residue 141 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 43) chain A residue 151 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 44) chain A residue 153 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 45) chain A residue 158 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 46) chain A residue 159 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 47) chain A residue 161 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 48) chain A residue 163 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI2 49) chain A residue 166 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 50) chain A residue 201 type BINDING sequence H description BINDING => ECO:0000269|PubMed:8740360 source Swiss-Prot : SWS_FT_FI3 51) chain A residue 205 type BINDING sequence H description BINDING => ECO:0000269|PubMed:8740360 source Swiss-Prot : SWS_FT_FI3 52) chain A residue 211 type BINDING sequence H description BINDING => ECO:0000269|PubMed:8740360 source Swiss-Prot : SWS_FT_FI3

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