eF-site ID 7acn-A PDB Code 7acn Chain A click to enlarge Title CRYSTAL STRUCTURES OF ACONITASE WITH ISOCITRATE AND NITROISOCITRATE BOUND Classification LYASE(CARBON-OXYGEN) Compound ACONITASE Source Sus scrofa (Pig) (ACON_PIG) Sequence A:  RAKVAMSHFEPHEYIRYDLLEKNIDIVRKRLNRPLTLSEK IVYGHLDDPANQEIERGKTYLRLRPDRVAMQDATAQMAML QFISSGLPKVAVPSTIHCDHLIEAQLGGEKDLRRAKDINQ EVYNFLATAGAKYGVGFWRPGSGIIHQIILENYAYPGVLL IGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPK VIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYH GPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLS KTGRADIANLADEFKDHLVPDPGCHYDQVIEINLSELKPH INGPFTPDLAHPVAEVGSVAEKEGWPLDIRVGLIGSCTNS SYEDMGRSAAVAKQALAHGLKCKSQFTITPGSEQIRATIE RDGYAQVLRDVGGIVLANACGPCIGQWDRKDIKKGEKNTI VTSYNRNFTGRNDANPETHAFVTSPEIVTALAIAGTLKFN PETDFLTGKDGKKFKLEAPDADELPRAEFDPGQDTYQHPP KDSSGQRVDVSPTSQRLQLLEPFDKWDGKDLEDLQILIKV KGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINIENRK ANSVRNAVTQEFGPVPDTARYYKQHGIRWVVIGDENYGEG SSREHSALEPRHLGGRAIITKSFARIHETNLKKQGLLPLT FADPADYNKIHPVDKLTIQGLKDFAPGKPLKCIIKHPNGT QETILLNHTFNETQIEWFRAGSALNRMKELQQK Description Functional site 1) chain A residue 72 type sequence Q description source : ACT 2) chain A residue 100 type sequence D description source : ACT 3) chain A residue 101 type sequence H description source : ACT 4) chain A residue 147 type sequence H description source : ACT 5) chain A residue 165 type sequence D description source : ACT 6) chain A residue 166 type sequence S description source : ACT 7) chain A residue 167 type sequence H description source : ACT 8) chain A residue 170 type sequence N description source : ACT 9) chain A residue 258 type sequence N description source : ACT 10) chain A residue 262 type sequence E description source : ACT 11) chain A residue 446 type sequence N description source : ACT 12) chain A residue 447 type sequence R description source : ACT 13) chain A residue 452 type sequence R description source : ACT 14) chain A residue 580 type sequence R description source : ACT 15) chain A residue 642 type sequence S description source : ACT 16) chain A residue 643 type sequence S description source : ACT 17) chain A residue 644 type sequence R description source : ACT 18) chain A residue 101 type sequence H description BINDING SITE FOR RESIDUE SF4 A 999 source : AC1 19) chain A residue 165 type sequence D description BINDING SITE FOR RESIDUE SF4 A 999 source : AC1 20) chain A residue 167 type sequence H description BINDING SITE FOR RESIDUE SF4 A 999 source : AC1 21) chain A residue 357 type sequence S description BINDING SITE FOR RESIDUE SF4 A 999 source : AC1 22) chain A residue 358 type sequence C description BINDING SITE FOR RESIDUE SF4 A 999 source : AC1 23) chain A residue 421 type sequence C description BINDING SITE FOR RESIDUE SF4 A 999 source : AC1 24) chain A residue 424 type sequence C description BINDING SITE FOR RESIDUE SF4 A 999 source : AC1 25) chain A residue 425 type sequence I description BINDING SITE FOR RESIDUE SF4 A 999 source : AC1 26) chain A residue 446 type sequence N description BINDING SITE FOR RESIDUE SF4 A 999 source : AC1 27) chain A residue 72 type sequence Q description BINDING SITE FOR RESIDUE ICT A 755 source : AC2 28) chain A residue 74 type sequence A description BINDING SITE FOR RESIDUE ICT A 755 source : AC2 29) chain A residue 101 type sequence H description BINDING SITE FOR RESIDUE ICT A 755 source : AC2 30) chain A residue 165 type sequence D description BINDING SITE FOR RESIDUE ICT A 755 source : AC2 31) chain A residue 166 type sequence S description BINDING SITE FOR RESIDUE ICT A 755 source : AC2 32) chain A residue 447 type sequence R description BINDING SITE FOR RESIDUE ICT A 755 source : AC2 33) chain A residue 452 type sequence R description BINDING SITE FOR RESIDUE ICT A 755 source : AC2 34) chain A residue 580 type sequence R description BINDING SITE FOR RESIDUE ICT A 755 source : AC2 35) chain A residue 642 type sequence S description BINDING SITE FOR RESIDUE ICT A 755 source : AC2 36) chain A residue 643 type sequence S description BINDING SITE FOR RESIDUE ICT A 755 source : AC2 37) chain A residue 644 type sequence R description BINDING SITE FOR RESIDUE ICT A 755 source : AC2 38) chain A residue 72 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10631981 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 165 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10631981 source Swiss-Prot : SWS_FT_FI1 40) chain A residue 447 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10631981 source Swiss-Prot : SWS_FT_FI1 41) chain A residue 452 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10631981 source Swiss-Prot : SWS_FT_FI1 42) chain A residue 580 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10631981 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 643 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10631981 source Swiss-Prot : SWS_FT_FI1 44) chain A residue 358 type BINDING sequence C description BINDING => ECO:0000269|PubMed:10631981, ECO:0000269|PubMed:2726740 source Swiss-Prot : SWS_FT_FI2 45) chain A residue 421 type BINDING sequence C description BINDING => ECO:0000269|PubMed:10631981, ECO:0000269|PubMed:2726740 source Swiss-Prot : SWS_FT_FI2 46) chain A residue 424 type BINDING sequence C description BINDING => ECO:0000269|PubMed:10631981, ECO:0000269|PubMed:2726740 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 643 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI7 48) chain A residue 532 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q99798 source Swiss-Prot : SWS_FT_FI6 49) chain A residue 4 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI4 50) chain A residue 384 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI4 51) chain A residue 522 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI4 52) chain A residue 550 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI4 53) chain A residue 564 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI4 54) chain A residue 601 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI4 55) chain A residue 662 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI4 56) chain A residue 23 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI5 57) chain A residue 703 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI5 58) chain A residue 111 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI5 59) chain A residue 117 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI5 60) chain A residue 206 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI5 61) chain A residue 490 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI5 62) chain A residue 496 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI5 63) chain A residue 546 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI5 64) chain A residue 578 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI5 65) chain A residue 696 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI5 66) chain A residue 709 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI8 67) chain A residue 712 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI8 68) chain A residue 716 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q99KI0 source Swiss-Prot : SWS_FT_FI8 69) chain A residue 173-186 type prosite sequence GLGGICIGVGGADA description THIOLASE_3 Thiolases active site. GLGGICIGvGgAdA source prosite : PS00099 70) chain A residue 350-366 type prosite sequence IRVGLIGSCTNSSYEDM description ACONITASE_1 Aconitase family signature 1. IrvGlIGSC.TNSsyedM source prosite : PS00450 71) chain A residue 413-426 type prosite sequence GGIVLANACGPCIG description ACONITASE_2 Aconitase family signature 2. GgiVlanACGPCIG source prosite : PS01244

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