eF-site ID 1b0j-A PDB Code 1b0j Chain A click to enlarge Title CRYSTAL STRUCTURE OF ACONITASE WITH ISOCITRATE Classification LYASE Compound ACONITATE HYDRATASE Source (ACON_PIG) Sequence A:  RAKVAMSHFEPHEYIRYDLLEKNIDIVRKRLNRPLTLSEK IVYGHLDDPANQEIERGKTYLRLRPDRVAMQDATAQMAML QFISSGLPKVAVPSTIHCDHLIEAQLGGEKDLRRAKDINQ EVYNFLATAGAKYGVGFWRPGSGIIHQIILENYAYPGVLL IGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPK VIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYH GPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLS KTGRADIANLADEFKDHLVPDPGCHYDQVIEINLSELKPH INGPFTPDLAHPVAEVGSVAEKEGWPLDIRVGLIGSCTNS SYEDMGRSAAVAKQALAHGLKCKSQFTITPGSEQIRATIE RDGYAQVLRDVGGIVLANACGPCIGQWDRKDIKKGEKNTI VTSYNRNFTGRNDANPETHAFVTSPEIVTALAIAGTLKFN PETDFLTGKDGKKFKLEAPDADELPRAEFDPGQDTYQHPP KDSSGQRVDVSPTSQRLQLLEPFDKWDGKDLEDLQILIKV KGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINIENRK ANSVRNAVTQEFGPVPDTARYYKQHGIRWVVIGDENYGEG ASREHSALEPRHLGGRAIITKSFARIHETNLKKQGLLPLT FADPADYNKIHPVDKLTIQGLKDFAPGKPLKCIIKHPNGT QETILLNHTFNETQIEWFRAGSALNRMKELQQK Description Functional site 1) chain A residue 167 type sequence H description BINDING SITE FOR RESIDUE SF4 A 755 source : AC1 2) chain A residue 357 type sequence S description BINDING SITE FOR RESIDUE SF4 A 755 source : AC1 3) chain A residue 358 type sequence C description BINDING SITE FOR RESIDUE SF4 A 755 source : AC1 4) chain A residue 421 type sequence C description BINDING SITE FOR RESIDUE SF4 A 755 source : AC1 5) chain A residue 424 type sequence C description BINDING SITE FOR RESIDUE SF4 A 755 source : AC1 6) chain A residue 425 type sequence I description BINDING SITE FOR RESIDUE SF4 A 755 source : AC1 7) chain A residue 446 type sequence N description BINDING SITE FOR RESIDUE SF4 A 755 source : AC1 8) chain A residue 72 type sequence Q description BINDING SITE FOR RESIDUE ICT A 756 source : AC2 9) chain A residue 101 type sequence H description BINDING SITE FOR RESIDUE ICT A 756 source : AC2 10) chain A residue 165 type sequence D description BINDING SITE FOR RESIDUE ICT A 756 source : AC2 11) chain A residue 166 type sequence S description BINDING SITE FOR RESIDUE ICT A 756 source : AC2 12) chain A residue 447 type sequence R description BINDING SITE FOR RESIDUE ICT A 756 source : AC2 13) chain A residue 452 type sequence R description BINDING SITE FOR RESIDUE ICT A 756 source : AC2 14) chain A residue 580 type sequence R description BINDING SITE FOR RESIDUE ICT A 756 source : AC2 15) chain A residue 642 type sequence A description BINDING SITE FOR RESIDUE ICT A 756 source : AC2 16) chain A residue 643 type sequence S description BINDING SITE FOR RESIDUE ICT A 756 source : AC2 17) chain A residue 644 type sequence R description BINDING SITE FOR RESIDUE ICT A 756 source : AC2 18) chain A residue 72 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10631981 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 165 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10631981 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 447 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10631981 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 452 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10631981 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 580 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10631981 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 643 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10631981 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 358 type BINDING sequence C description BINDING => ECO:0000269|PubMed:10631981, ECO:0000269|PubMed:2726740 source Swiss-Prot : SWS_FT_FI2 25) chain A residue 421 type BINDING sequence C description BINDING => ECO:0000269|PubMed:10631981, ECO:0000269|PubMed:2726740 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 424 type BINDING sequence C description BINDING => ECO:0000269|PubMed:10631981, ECO:0000269|PubMed:2726740 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 709 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI8 28) chain A residue 712 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI8 29) chain A residue 716 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI8 30) chain A residue 4 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI4 31) chain A residue 384 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI4 32) chain A residue 522 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI4 33) chain A residue 550 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI4 34) chain A residue 564 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI4 35) chain A residue 601 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI4 36) chain A residue 662 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI4 37) chain A residue 23 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI5 38) chain A residue 703 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI5 39) chain A residue 111 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI5 40) chain A residue 117 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI5 41) chain A residue 206 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI5 42) chain A residue 490 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI5 43) chain A residue 496 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI5 44) chain A residue 546 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI5 45) chain A residue 578 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI5 46) chain A residue 696 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI5 47) chain A residue 532 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q99798 source Swiss-Prot : SWS_FT_FI6 48) chain A residue 643 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI7 49) chain A residue 173-186 type prosite sequence GLGGICIGVGGADA description THIOLASE_3 Thiolases active site. GLGGICIGvGgAdA source prosite : PS00099 50) chain A residue 350-366 type prosite sequence IRVGLIGSCTNSSYEDM description ACONITASE_1 Aconitase family signature 1. IrvGlIGSC.TNSsyedM source prosite : PS00450 51) chain A residue 413-426 type prosite sequence GGIVLANACGPCIG description ACONITASE_2 Aconitase family signature 2. GgiVlanACGPCIG source prosite : PS01244

Display surface Download Links