eF-site ID 3gzj-ABCDE PDB Code 3gzj Chain A, B, C, D, E click to enlarge Title Crystal Structure of Polyneuridine Aldehyde Esterase Complexed with 16-epi-Vellosimine Classification HYDROLASE Compound Polyneuridine-aldehyde esterase Source null (PNAE_RAUSE) Sequence A:  QKHFVLVHGGCLGAWIWYKLKPLLESAGHKVTAVDLSAAG INPRRLDEIHTFRDYSEPLMEVMASIPPDEKVVLLGHSFG GMSLGLAMETYPEKISVAVFMSAMMPDPNHSLTYPFEKYN EKCPADMMLDSQFSTYGNPENPGMSMILGPQFMALKMFQN CSVEDLELAKMLTRPGSLFFQDLAKAKKFSTERYGSVKRA YIFCNEDKSFPVEFQKWFVESVGADKVKEIKEADAMGMLS QPREVCKCLLDISD B:  QKHFVLVHGGCLGAWIWYKLKPLLESAGHKVTAVDLSAAG INPRRLDEIHTFRDYSEPLMEVMASIPPDEKVVLLGHSFG GMSLGLAMETYPEKISVAVFMSAMMPDPNHSLTYPFEKYN EKCPADMMLDSQFSTYGNPENPGMSMILGPQFMALKMFQN CSVEDLELAKMLTRPGSLFFQDLAKAKKFSTERYGSVKRA YIFCNEDKSFPVEFQKWFVESVGADKVKEIKEADAMGMLS QPREVCKCLLDISD C:  QKHFVLVHGGCLGAWIWYKLKPLLESAGHKVTAVDLSAAG INPRRLDEIHTFRDYSEPLMEVMASIPPDEKVVLLGHSFG GMSLGLAMETYPEKISVAVFMSAMMPDPNHSLTYPFEKYN EKCPADMMLDSQFSTYGNPENPGMSMILGPQFMALKMFQN CSVEDLELAKMLTRPGSLFFQDLAKAKKFSTERYGSVKRA YIFCNEDKSFPVEFQKWFVESVGADKVKEIKEADAMGMLS QPREVCKCLLDISD D:  QKHFVLVHGGCLGAWIWYKLKPLLESAGHKVTAVDLSAAG INPRRLDEIHTFRDYSEPLMEVMASIPPDEKVVLLGHSFG GMSLGLAMETYPEKISVAVFMSAMMPDPNHSLTYPFEKYN EKCPADMMLDSQFSTYGNPENPGMSMILGPQFMALKMFQN CSVEDLELAKMLTRPGSLFFQDLAKAKKFSTERYGSVKRA YIFCNEDKSFPVEFQKWFVESVGADKVKEIKEADAMGMLS QPREVCKCLLDISD E:  QKHFVLVHGGCLGAWIWYKLKPLLESAGHKVTAVDLSAAG INPRRLDEIHTFRDYSEPLMEVMASIPPDEKVVLLGHSFG GMSLGLAMETYPEKISVAVFMSAMMPDPNHSLTYPFEKYN EKCPADMMLDSQFSTYGNPENPGMSMILGPQFMALKMFQN CSVEDLELAKMLTRPGSLFFQDLAKAKKFSTERYGSVKRA YIFCNEDKSFPVEFQKWFVESVGADKVKEIKEADAMGMLS QPREVCKCLLDISD Description Functional site 1) chain A residue 19 type sequence G description BINDING SITE FOR RESIDUE EVS A 1000 source : AC1 2) chain A residue 87 type sequence S description BINDING SITE FOR RESIDUE EVS A 1000 source : AC1 3) chain A residue 88 type sequence F description BINDING SITE FOR RESIDUE EVS A 1000 source : AC1 4) chain A residue 113 type sequence M description BINDING SITE FOR RESIDUE EVS A 1000 source : AC1 5) chain A residue 124 type sequence P description BINDING SITE FOR RESIDUE EVS A 1000 source : AC1 6) chain A residue 128 type sequence Y description BINDING SITE FOR RESIDUE EVS A 1000 source : AC1 7) chain A residue 155 type sequence M description BINDING SITE FOR RESIDUE EVS A 1000 source : AC1 8) chain A residue 187 type sequence L description BINDING SITE FOR RESIDUE EVS A 1000 source : AC1 9) chain B residue 19 type sequence G description BINDING SITE FOR RESIDUE EVS B 1000 source : AC2 10) chain B residue 87 type sequence S description BINDING SITE FOR RESIDUE EVS B 1000 source : AC2 11) chain B residue 88 type sequence F description BINDING SITE FOR RESIDUE EVS B 1000 source : AC2 12) chain B residue 113 type sequence M description BINDING SITE FOR RESIDUE EVS B 1000 source : AC2 13) chain B residue 124 type sequence P description BINDING SITE FOR RESIDUE EVS B 1000 source : AC2 14) chain B residue 125 type sequence F description BINDING SITE FOR RESIDUE EVS B 1000 source : AC2 15) chain B residue 128 type sequence Y description BINDING SITE FOR RESIDUE EVS B 1000 source : AC2 16) chain B residue 137 type sequence M description BINDING SITE FOR RESIDUE EVS B 1000 source : AC2 17) chain B residue 187 type sequence L description BINDING SITE FOR RESIDUE EVS B 1000 source : AC2 18) chain C residue 19 type sequence G description BINDING SITE FOR RESIDUE EVS C 1000 source : AC3 19) chain C residue 87 type sequence S description BINDING SITE FOR RESIDUE EVS C 1000 source : AC3 20) chain C residue 88 type sequence F description BINDING SITE FOR RESIDUE EVS C 1000 source : AC3 21) chain C residue 113 type sequence M description BINDING SITE FOR RESIDUE EVS C 1000 source : AC3 22) chain C residue 125 type sequence F description BINDING SITE FOR RESIDUE EVS C 1000 source : AC3 23) chain C residue 128 type sequence Y description BINDING SITE FOR RESIDUE EVS C 1000 source : AC3 24) chain C residue 155 type sequence M description BINDING SITE FOR RESIDUE EVS C 1000 source : AC3 25) chain C residue 157 type sequence L description BINDING SITE FOR RESIDUE EVS C 1000 source : AC3 26) chain C residue 187 type sequence L description BINDING SITE FOR RESIDUE EVS C 1000 source : AC3 27) chain D residue 19 type sequence G description BINDING SITE FOR RESIDUE EVS D 1000 source : AC4 28) chain D residue 87 type sequence S description BINDING SITE FOR RESIDUE EVS D 1000 source : AC4 29) chain D residue 88 type sequence F description BINDING SITE FOR RESIDUE EVS D 1000 source : AC4 30) chain D residue 113 type sequence M description BINDING SITE FOR RESIDUE EVS D 1000 source : AC4 31) chain D residue 124 type sequence P description BINDING SITE FOR RESIDUE EVS D 1000 source : AC4 32) chain D residue 125 type sequence F description BINDING SITE FOR RESIDUE EVS D 1000 source : AC4 33) chain D residue 128 type sequence Y description BINDING SITE FOR RESIDUE EVS D 1000 source : AC4 34) chain D residue 137 type sequence M description BINDING SITE FOR RESIDUE EVS D 1000 source : AC4 35) chain D residue 157 type sequence L description BINDING SITE FOR RESIDUE EVS D 1000 source : AC4 36) chain B residue 87 type ACT_SITE sequence S description ACT_SITE => ECO:0000269|PubMed:12071952 source Swiss-Prot : SWS_FT_FI1 37) chain B residue 216 type ACT_SITE sequence D description ACT_SITE => ECO:0000269|PubMed:12071952 source Swiss-Prot : SWS_FT_FI1 38) chain B residue 244 type ACT_SITE sequence A description ACT_SITE => ECO:0000269|PubMed:12071952 source Swiss-Prot : SWS_FT_FI1 39) chain C residue 87 type ACT_SITE sequence S description ACT_SITE => ECO:0000269|PubMed:12071952 source Swiss-Prot : SWS_FT_FI1 40) chain C residue 216 type ACT_SITE sequence D description ACT_SITE => ECO:0000269|PubMed:12071952 source Swiss-Prot : SWS_FT_FI1 41) chain C residue 244 type ACT_SITE sequence A description ACT_SITE => ECO:0000269|PubMed:12071952 source Swiss-Prot : SWS_FT_FI1 42) chain D residue 87 type ACT_SITE sequence S description ACT_SITE => ECO:0000269|PubMed:12071952 source Swiss-Prot : SWS_FT_FI1 43) chain D residue 216 type ACT_SITE sequence D description ACT_SITE => ECO:0000269|PubMed:12071952 source Swiss-Prot : SWS_FT_FI1 44) chain D residue 244 type ACT_SITE sequence A description ACT_SITE => ECO:0000269|PubMed:12071952 source Swiss-Prot : SWS_FT_FI1 45) chain E residue 87 type ACT_SITE sequence S description ACT_SITE => ECO:0000269|PubMed:12071952 source Swiss-Prot : SWS_FT_FI1 46) chain E residue 216 type ACT_SITE sequence D description ACT_SITE => ECO:0000269|PubMed:12071952 source Swiss-Prot : SWS_FT_FI1 47) chain E residue 244 type ACT_SITE sequence A description ACT_SITE => ECO:0000269|PubMed:12071952 source Swiss-Prot : SWS_FT_FI1 48) chain A residue 87 type ACT_SITE sequence S description ACT_SITE => ECO:0000269|PubMed:12071952 source Swiss-Prot : SWS_FT_FI1 49) chain A residue 216 type ACT_SITE sequence D description ACT_SITE => ECO:0000269|PubMed:12071952 source Swiss-Prot : SWS_FT_FI1 50) chain A residue 244 type ACT_SITE sequence A description ACT_SITE => ECO:0000269|PubMed:12071952 source Swiss-Prot : SWS_FT_FI1 51) chain D residue 87 type BINDING sequence S description covalent => ECO:0000269|PubMed:19496101, ECO:0007744|PDB:3GZJ source Swiss-Prot : SWS_FT_FI2 52) chain E residue 87 type BINDING sequence S description covalent => ECO:0000269|PubMed:19496101, ECO:0007744|PDB:3GZJ source Swiss-Prot : SWS_FT_FI2 53) chain A residue 87 type BINDING sequence S description covalent => ECO:0000269|PubMed:19496101, ECO:0007744|PDB:3GZJ source Swiss-Prot : SWS_FT_FI2 54) chain B residue 87 type BINDING sequence S description covalent => ECO:0000269|PubMed:19496101, ECO:0007744|PDB:3GZJ source Swiss-Prot : SWS_FT_FI2 55) chain C residue 87 type BINDING sequence S description covalent => ECO:0000269|PubMed:19496101, ECO:0007744|PDB:3GZJ source Swiss-Prot : SWS_FT_FI2 56) chain A residue 81-90 type prosite sequence VVLLGHSFGG description LIPASE_SER Lipases, serine active site. VVLLGHSFGG source prosite : PS00120

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