eF-site ID 1o8u-ABCDEF PDB Code 1o8u Chain A, B, C, D, E, F click to enlarge Title The 2 Angstrom Structure of 6-Oxo Camphor Hydrolase: New Structural Diversity in the Crotonase Superfamily Classification HYDROLASE Compound 6-OXO CAMPHOR HYDROLASE Source (Q93TU6) Sequence A:  LATPFQEYSQKYENIRLERDGGVLLVTVHTEGKSLVWTST AHDELAYCFHDIACDRENKVVILTGTGPSFCNEIDFTSFN LGTPHDWDEIIFEGQRLLNNLLSIEVPVIAAVNGPVTNHP EIPVMSDIVLAAESATFQDGPHFPSGIVPGDGAHVVWPHV LGSNRGRYFLLTGQELDARTALDYGAVNEVLSEQELLPRA WELARGIAEKPLLARRYARKVLTRQLRRVMEADLSLGLAH EALAAIDLG B:  LATPFQEYSQKYENIRLERDGGVLLVTVHTEGKSLVWTST AHDELAYCFHDIACDRENKVVILTGTGPSFCNEIDFTSFN LGTPHDWDEIIFEGQRLLNNLLSIEVPVIAAVNGPVTNHP EIPVMSDIVLAAESATFQDGPHFPSGIVPGDGAHVVWPHV LGSNRGRYFLLTGQELDARTALDYGAVNEVLSEQELLPRA WELARGIAEKPLLARRYARKVLTRQLRRVMEADLSLGLAH EALAAIDLG C:  TPFQEYSQKYENIRLERDGGVLLVTVHTEGKSLVWTSTAH DELAYCFHDIACDRENKVVILTGTGPSFCNEIDFTSFNLG TPHDWDEIIFEGQRLLNNLLSIEVPVIAAVNGPVTNHPEI PVMSDIVLAAESATFQDGPHFPSGIVPGDGAHVVWPHVLG SNRGRYFLLTGQELDARTALDYGAVNEVLSEQELLPRAWE LARGIAEKPLLARRYARKVLTRQLRRVMEADLSLGLAHEA LAAIDLG D:  TPFQEYSQKYENIRLERDGGVLLVTVHTEGKSLVWTSTAH DELAYCFHDIACDRENKVVILTGTGPSFCNEIDFTSFNLG TPHDWDEIIFEGQRLLNNLLSIEVPVIAAVNGPVTNHPEI PVMSDIVLAAESATFQDGPHFPSGIVPGDGAHVVWPHVLG SNRGRYFLLTGQELDARTALDYGAVNEVLSEQELLPRAWE LARGIAEKPLLARRYARKVLTRQLRRVMEADLSLGLAHEA LAAIDLG E:  LATPFQEYSQKYENIRLERDGGVLLVTVHTEGKSLVWTST AHDELAYCFHDIACDRENKVVILTGTGPSFCNEIDFTSFN LGTPHDWDEIIFEGQRLLNNLLSIEVPVIAAVNGPVTNHP EIPVMSDIVLAAESATFQDGPHFPSGIVPGDGAHVVWPHV LGSNRGRYFLLTGQELDARTALDYGAVNEVLSEQELLPRA WELARGIAEKPLLARRYARKVLTRQLRRVMEADLSLGLAH EALAAIDLG F:  ATPFQEYSQKYENIRLERDGGVLLVTVHTEGKSLVWTSTA HDELAYCFHDIACDRENKVVILTGTGPSFCNEIDFTSFNL GTPHDWDEIIFEGQRLLNNLLSIEVPVIAAVNGPVTNHPE IPVMSDIVLAAESATFQDGPHFPSGIVPGDGAHVVWPHVL GSNRGRYFLLTGQELDARTALDYGAVNEVLSEQELLPRAW ELARGIAEKPLLARRYARKVLTRQLRRVMEADLSLGLAHE ALAAIDLG Description (1)  6-OXO CAMPHOR HYDROLASE Functional site 1) chain B residue 186 type sequence D description BINDING SITE FOR RESIDUE NA A1253 source : AC1 2) chain C residue 186 type sequence D description BINDING SITE FOR RESIDUE NA A1253 source : AC1 3) chain E residue 186 type sequence D description BINDING SITE FOR RESIDUE NA D1253 source : AC2 4) chain A residue 40 type BINDING sequence W description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 5) chain C residue 145 type BINDING sequence H description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 6) chain C residue 154 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 7) chain C residue 244 type BINDING sequence E description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 8) chain D residue 40 type BINDING sequence W description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 9) chain D residue 145 type BINDING sequence H description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 10) chain D residue 154 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 11) chain D residue 244 type BINDING sequence E description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 12) chain E residue 40 type BINDING sequence W description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 13) chain E residue 145 type BINDING sequence H description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 14) chain E residue 154 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 145 type BINDING sequence H description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 16) chain E residue 244 type BINDING sequence E description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 17) chain F residue 40 type BINDING sequence W description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 18) chain F residue 145 type BINDING sequence H description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 19) chain F residue 154 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 20) chain F residue 244 type BINDING sequence E description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 154 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 244 type BINDING sequence E description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 23) chain B residue 40 type BINDING sequence W description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 24) chain B residue 145 type BINDING sequence H description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 25) chain B residue 154 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 26) chain B residue 244 type BINDING sequence E description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 27) chain C residue 40 type BINDING sequence W description BINDING => ECO:0000269|PubMed:15138275 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 124 type ACT_SITE sequence E description Nucleophile => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 124 type ACT_SITE sequence E description Nucleophile => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 30) chain C residue 124 type ACT_SITE sequence E description Nucleophile => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 31) chain D residue 124 type ACT_SITE sequence E description Nucleophile => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 32) chain E residue 124 type ACT_SITE sequence E description Nucleophile => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 33) chain F residue 124 type ACT_SITE sequence E description Nucleophile => ECO:0000250 source Swiss-Prot : SWS_FT_FI1

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