eF-site ID 3geb-ABCD PDB Code 3geb Chain A, B, C, D click to enlarge Title Crystal Structure of edeya2 Classification HYDROLASE Compound Eyes absent homolog 2 Source null (EYA2_HUMAN) Sequence A:  SHMERVFVWDLDETIIIFHSLLTGTFASRYGKDTTTSVRI GLMMEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQD LSTYNFSADGFGGVDWMRKLAFRYRRVKEMYNTYKNNVGG LIGTPKRETWLQLRAELEALTDLWLTHSLKALNLINSRPN CVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKTGK ESCFERIMQRFGRKAVYVVIGDGVEEEQGAKKHNMPFWRI SCHADLEALRHALELEYL B:  ERVFVWDLDETIIIFHSLLTGTFASRYGKDTTTSVRIGLM MEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQDLST YNFSADGFHDWMRKLAFRYRRVKEMYNTYKNNVGGLIGTP KRETWLQLRAELEALTDLWLTHSLKALNLINSRPNCVNVL VTTTQLIPALAKVLLYGLGSVFPIENIYSATKTGKESCFE RIMQRFGRKAVYVVIGDGVEEEQGAKKHNMPFWRISCHAD LEALRHALELEYL C:  SHMERVFVWDLDETIIIFHSLLTGTFASRYGKDTTTSVRI GLMMEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQD LSTYNFSADGFGGVDWMRKLAFRYRRVKEMYNTYKNNVGG LIGTPKRETWLQLRAELEALTDLWLTHSLKALNLINSRPN CVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKTGK ESCFERIMQRFGRKAVYVVIGDGVEEEQGAKKHNMPFWRI SCHADLEALRHALELEYL D:  ERVFVWDLDETIIIFHSLLTGTFASRYGKDTTTSVRIGLM MEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQDLST YNFSADGFHGGVDWMRKLAFRYRRVKEMYNTYKNNVGGLI GTPKRETWLQLRAELEALTDLWLTHSLKALNLINSRPNCV NVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKTGKES CFERIMQRFGRKAVYVVIGDGVEEEQGAKKHNMPFWRISC HADLEALRHALELEYL Description Functional site 1) chain A residue 274 type sequence D description BINDING SITE FOR RESIDUE MG A 701 source : AC1 2) chain A residue 276 type sequence D description BINDING SITE FOR RESIDUE MG A 701 source : AC1 3) chain A residue 502 type sequence D description BINDING SITE FOR RESIDUE MG A 701 source : AC1 4) chain B residue 274 type sequence D description BINDING SITE FOR RESIDUE MG B 702 source : AC2 5) chain B residue 276 type sequence D description BINDING SITE FOR RESIDUE MG B 702 source : AC2 6) chain B residue 502 type sequence D description BINDING SITE FOR RESIDUE MG B 702 source : AC2 7) chain C residue 274 type sequence D description BINDING SITE FOR RESIDUE MG C 703 source : AC3 8) chain C residue 276 type sequence D description BINDING SITE FOR RESIDUE MG C 703 source : AC3 9) chain C residue 502 type sequence D description BINDING SITE FOR RESIDUE MG C 703 source : AC3 10) chain D residue 274 type sequence D description BINDING SITE FOR RESIDUE MG D 704 source : AC4 11) chain D residue 276 type sequence D description BINDING SITE FOR RESIDUE MG D 704 source : AC4 12) chain D residue 502 type sequence D description BINDING SITE FOR RESIDUE MG D 704 source : AC4 13) chain A residue 274 type ACT_SITE sequence D description Nucleophile => ECO:0000269|PubMed:19858093 source Swiss-Prot : SWS_FT_FI1 14) chain B residue 274 type ACT_SITE sequence D description Nucleophile => ECO:0000269|PubMed:19858093 source Swiss-Prot : SWS_FT_FI1 15) chain C residue 274 type ACT_SITE sequence D description Nucleophile => ECO:0000269|PubMed:19858093 source Swiss-Prot : SWS_FT_FI1 16) chain D residue 274 type ACT_SITE sequence D description Nucleophile => ECO:0000269|PubMed:19858093 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 276 type ACT_SITE sequence D description Proton donor => ECO:0000269|PubMed:19858093 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 276 type ACT_SITE sequence D description Proton donor => ECO:0000269|PubMed:19858093 source Swiss-Prot : SWS_FT_FI2 19) chain C residue 276 type ACT_SITE sequence D description Proton donor => ECO:0000269|PubMed:19858093 source Swiss-Prot : SWS_FT_FI2 20) chain D residue 276 type ACT_SITE sequence D description Proton donor => ECO:0000269|PubMed:19858093 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19351884 source Swiss-Prot : SWS_FT_FI3 22) chain D residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19351884 source Swiss-Prot : SWS_FT_FI3 23) chain D residue 276 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19351884 source Swiss-Prot : SWS_FT_FI3 24) chain D residue 502 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19351884 source Swiss-Prot : SWS_FT_FI3 25) chain C residue 502 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19351884 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 276 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19351884 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 502 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19351884 source Swiss-Prot : SWS_FT_FI3 28) chain B residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19351884 source Swiss-Prot : SWS_FT_FI3 29) chain B residue 276 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19351884 source Swiss-Prot : SWS_FT_FI3 30) chain B residue 502 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19351884 source Swiss-Prot : SWS_FT_FI3 31) chain C residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19351884 source Swiss-Prot : SWS_FT_FI3 32) chain C residue 276 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19351884 source Swiss-Prot : SWS_FT_FI3

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