eF-site ID 3ba0-A PDB Code 3ba0 Chain A click to enlarge Title Crystal structure of full-length human MMP-12 Classification HYDROLASE Compound Macrophage metalloelastase Source (MMP12_HUMAN) Sequence A:  GPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVT PLKFSKINTGMADILVVFARGAHGDDHAFDGKGGILAHAF GPGSGIGGDAHFDEDEFWTTHSGGTNLFLTAVHEIGHSLG LGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSLYGDP KENQRLPNPDNSEPALCDPNLSFDAVTTVGNKIFFFKDRF FWLKVSERPKTSVNLISSLWPTLPSGIEAAYEIEARNQVF LFKDDKYWLISNLRPEPNYPKSIHSFGFPNFVKKIDAAVF NPRFYRTYFFVDNQYWRYDERRQMMDPGYPKLITKNFQGI GPKIDAVFYSKNKYYYFFQGSNQFEYDFLLQRITKTLKSN SWFGC Description Functional site 1) chain A residue 218 type sequence H description BINDING SITE FOR RESIDUE ZN A 471 source : AC1 2) chain A residue 219 type sequence E description BINDING SITE FOR RESIDUE ZN A 471 source : AC1 3) chain A residue 222 type sequence H description BINDING SITE FOR RESIDUE ZN A 471 source : AC1 4) chain A residue 228 type sequence H description BINDING SITE FOR RESIDUE ZN A 471 source : AC1 5) chain A residue 168 type sequence H description BINDING SITE FOR RESIDUE ZN A 472 source : AC2 6) chain A residue 170 type sequence D description BINDING SITE FOR RESIDUE ZN A 472 source : AC2 7) chain A residue 183 type sequence H description BINDING SITE FOR RESIDUE ZN A 472 source : AC2 8) chain A residue 196 type sequence H description BINDING SITE FOR RESIDUE ZN A 472 source : AC2 9) chain A residue 158 type sequence D description BINDING SITE FOR RESIDUE CA A 473 source : AC3 10) chain A residue 192 type sequence G description BINDING SITE FOR RESIDUE CA A 473 source : AC3 11) chain A residue 194 type sequence D description BINDING SITE FOR RESIDUE CA A 473 source : AC3 12) chain A residue 124 type sequence D description BINDING SITE FOR RESIDUE CA A 474 source : AC4 13) chain A residue 199 type sequence E description BINDING SITE FOR RESIDUE CA A 474 source : AC4 14) chain A residue 201 type sequence E description BINDING SITE FOR RESIDUE CA A 474 source : AC4 15) chain A residue 175 type sequence D description BINDING SITE FOR RESIDUE CA A 475 source : AC5 16) chain A residue 176 type sequence G description BINDING SITE FOR RESIDUE CA A 475 source : AC5 17) chain A residue 178 type sequence G description BINDING SITE FOR RESIDUE CA A 475 source : AC5 18) chain A residue 180 type sequence I description BINDING SITE FOR RESIDUE CA A 475 source : AC5 19) chain A residue 198 type sequence D description BINDING SITE FOR RESIDUE CA A 475 source : AC5 20) chain A residue 201 type sequence E description BINDING SITE FOR RESIDUE CA A 475 source : AC5 21) chain A residue 289 type sequence D description BINDING SITE FOR RESIDUE CA A 476 source : AC6 22) chain A residue 333 type sequence E description BINDING SITE FOR RESIDUE CA A 476 source : AC6 23) chain A residue 381 type sequence D description BINDING SITE FOR RESIDUE CA A 476 source : AC6 24) chain A residue 430 type sequence D description BINDING SITE FOR RESIDUE CA A 476 source : AC6 25) chain A residue 182 type sequence A description BINDING SITE FOR RESIDUE HAE A 477 source : AC7 26) chain A residue 219 type sequence E description BINDING SITE FOR RESIDUE HAE A 477 source : AC7 27) chain A residue 222 type sequence H description BINDING SITE FOR RESIDUE HAE A 477 source : AC7 28) chain A residue 321-336 type prosite sequence ISSLWPTLPSGIEAAY description HEMOPEXIN Hemopexin domain signature. ISslWptlPsGIEAAY source prosite : PS00024 29) chain A residue 215-224 type prosite sequence TAVHEIGHSL description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAVHEIGHSL source prosite : PS00142 30) chain A residue 124 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 31) chain A residue 190 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 32) chain A residue 192 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 33) chain A residue 194 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 34) chain A residue 196 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 35) chain A residue 198 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 36) chain A residue 199 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 37) chain A residue 201 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 38) chain A residue 218 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 39) chain A residue 222 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 40) chain A residue 228 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 41) chain A residue 158 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 42) chain A residue 168 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 43) chain A residue 170 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 44) chain A residue 175 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 45) chain A residue 176 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 46) chain A residue 178 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 47) chain A residue 180 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI2 48) chain A residue 183 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 49) chain A residue 289 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 50) chain A residue 333 type BINDING sequence E description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 51) chain A residue 381 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 52) chain A residue 430 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 53) chain A residue 285 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 54) chain A residue 219 type ACT_SITE sequence E description source Swiss-Prot : SWS_FT_FI1

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