eF-site ID 2y3u-A PDB Code 2y3u Chain A click to enlarge Title Crystal structure of apo collagenase G from Clostridium histolyticum at 2.55 Angstrom resolution Classification HYDROLASE Compound COLLAGENASE Source null (Q9X721_CLOHI) Sequence A:  NLYFQGGTXYDFEYLNGLSYTELTNLIKNIKWNQINGLFN YSTGSQKFFGDKNRVQAIINALQESGRTYTANDXKGIETF TEVLRAGFYLGYYNDGLSYLNDRNFQDKCIPAXIAIQKNP NFKLGTAVQDEVITSLGKLIGNASANAEVVNNCVPVLKQF RENLNQYAPDYVKGTAVNELIKGIEFDFSGAAYEKDVKTX PWYGKIDPFINELKALGLYGNITSATEWASDVGIYYLSKF GLYSTNRNDIVQSLEKAVDXYKYGKIAFVAXERITWDYDG IGSNGKKVDHDKFLDDAEKHYLPKTYTFDNGTFIIRAGDK VSEEKIKRLYWASREVKSQFHRVVGNDKALEVGNADDVLT XKIFNSPEEYKFNTNINGVSTDNGGLYIEPRGTFYTYERT PQQSIFSLEELFRHEYTHYLQARYLVDGLWGQGPFYEKNR LTWFDEGTAEFFAGSTRTSGVLPRKLILGYLAKDKVDHRY SLKKTLNSDDSDWXFYNYGFAVAHYLYEKDXPTFIKXNKA ILNTDVKSYDEIIKKLSDDANKNTEYQNHIQELVDKYQGA GIPLVSDDYLKDHGYKKASEVYSEISKAASLTNTSVTAEK SQYFNTFTLRGTYTGETSKGEFKDWDEXSKKLDGTLESLA KNSWSGYKTLTAYFTNYRVTSDNKVQYDVVFHGVLTDNG Description (1)  COLLAGENASE (E.C.3.4.24.3) Functional site 1) chain A residue 277 type sequence A description BINDING SITE FOR RESIDUE P6G A 1792 source : AC1 2) chain A residue 278 type sequence P description BINDING SITE FOR RESIDUE P6G A 1792 source : AC1 3) chain A residue 280 type sequence Y description BINDING SITE FOR RESIDUE P6G A 1792 source : AC1 4) chain A residue 287 type sequence N description BINDING SITE FOR RESIDUE P6G A 1792 source : AC1 5) chain A residue 341 type sequence V description BINDING SITE FOR RESIDUE P6G A 1792 source : AC1 6) chain A residue 568 type sequence S description BINDING SITE FOR RESIDUE FLC A 1793 source : AC2 7) chain A residue 618 type sequence Y description BINDING SITE FOR RESIDUE FLC A 1793 source : AC2 8) chain A residue 622 type sequence X description BINDING SITE FOR RESIDUE FLC A 1793 source : AC2 9) chain A residue 736 type sequence W description BINDING SITE FOR RESIDUE FLC A 1793 source : AC2 10) chain A residue 737 type sequence D description BINDING SITE FOR RESIDUE FLC A 1793 source : AC2 11) chain A residue 740 type sequence S description BINDING SITE FOR RESIDUE FLC A 1793 source : AC2 12) chain A residue 524 type ACT_SITE sequence E description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:11121400 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 498 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q899Y1, ECO:0000303|PubMed:23703618 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 531 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:Q899Y1, ECO:0000303|PubMed:23703618 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 535 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:Q899Y1, ECO:0000303|PubMed:23703618 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 537 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q899Y1, ECO:0000303|PubMed:23703618 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 520-529 type prosite sequence LFRHEYTHYL description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. LFRHEYTHYL source prosite : PS00142 18) chain A residue 523 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:21947205, ECO:0000269|PubMed:23703618, ECO:0007744|PDB:2Y50, ECO:0007744|PDB:2Y6I, ECO:0007744|PDB:4ARE source Swiss-Prot : SWS_FT_FI3 19) chain A residue 527 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:21947205, ECO:0000269|PubMed:23703618, ECO:0007744|PDB:2Y50, ECO:0007744|PDB:2Y6I, ECO:0007744|PDB:4ARE source Swiss-Prot : SWS_FT_FI3 20) chain A residue 555 type BINDING sequence E description BINDING => ECO:0000269|PubMed:21947205, ECO:0000269|PubMed:23703618, ECO:0007744|PDB:2Y50, ECO:0007744|PDB:2Y6I, ECO:0007744|PDB:4ARE source Swiss-Prot : SWS_FT_FI4

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