eF-site ID 6f4l-A PDB Code 6f4l Chain A click to enlarge Title Structure of quinolinate synthase with inhibitor-derived quinolinate Classification TRANSFERASE Compound Quinolinate synthase A Source Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) (NADA_THEMA) Sequence A:  HHHHMVDEILKLKKEKGYIILAHNYQIPELQDIADFVGDS LQLARKAMELSEKKILFLGVDFMAELVKILNPDKKVIVPD RSATCPMANRLTPEIIREYREKFPDAPVVLYVNSTSECKT LADVICTSANAVEVVKKLDSSVVIFGPDRNLGEYVAEKTG KKVITIPENGHCPVHQFNAESIDAVRKKYPDAKVIVHPEC PKPVRDKADYVGSTGQMEKIPERDPSRIFVIGTEIGMIHK LKKKFPDREFVPLEMAVCVNMKKNTLENTLHALQTESFEV ILPKEVIEKAKKPILRMFELMG Description Functional site 1) chain A residue 81 type sequence C description binding site for residue SF4 A 301 source : AC1 2) chain A residue 83 type sequence M description binding site for residue SF4 A 301 source : AC1 3) chain A residue 168 type sequence C description binding site for residue SF4 A 301 source : AC1 4) chain A residue 169 type sequence P description binding site for residue SF4 A 301 source : AC1 5) chain A residue 195 type sequence E description binding site for residue SF4 A 301 source : AC1 6) chain A residue 254 type sequence C description binding site for residue SF4 A 301 source : AC1 7) chain A residue 19 type sequence H description binding site for residue NTM A 302 source : AC2 8) chain A residue 21 type sequence Y description binding site for residue NTM A 302 source : AC2 9) chain A residue 35 type sequence D description binding site for residue NTM A 302 source : AC2 10) chain A residue 36 type sequence S description binding site for residue NTM A 302 source : AC2 11) chain A residue 107 type sequence Y description binding site for residue NTM A 302 source : AC2 12) chain A residue 193 type sequence H description binding site for residue NTM A 302 source : AC2 13) chain A residue 195 type sequence E description binding site for residue NTM A 302 source : AC2 14) chain A residue 209 type sequence S description binding site for residue NTM A 302 source : AC2 15) chain A residue 210 type sequence T description binding site for residue NTM A 302 source : AC2 16) chain A residue 69 type sequence D description binding site for residue CL A 303 source : AC3 17) chain A residue 103 type sequence P description binding site for residue NHE A 304 source : AC4 18) chain A residue 135 type sequence D description binding site for residue NHE A 304 source : AC4 19) chain A residue 136 type sequence S description binding site for residue NHE A 304 source : AC4 20) chain A residue 292 type sequence R description binding site for residue NHE A 304 source : AC4 21) chain A residue 107 type BINDING sequence Y description BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000305|PubMed:27545412, ECO:0000305|PubMed:29641168 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 193 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000305|PubMed:27545412, ECO:0000305|PubMed:29641168, ECO:0000305|PubMed:30855610 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 210 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000305|PubMed:27545412, ECO:0000305|PubMed:29641168, ECO:0000305|PubMed:30855610 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 19 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000305|PubMed:27545412, ECO:0000305|PubMed:29641168, ECO:0000305|PubMed:30855610 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 36 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000305|PubMed:27545412, ECO:0000305|PubMed:29641168, ECO:0000305|PubMed:30855610 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 124 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000305|PubMed:27545412, ECO:0000305|PubMed:29641168, ECO:0000305|PubMed:30855610 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 168 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000269|PubMed:24650327, ECO:0000269|PubMed:27545412, ECO:0000269|PubMed:29641168, ECO:0007744|PDB:4P3X, ECO:0007744|PDB:5F33, ECO:0007744|PDB:5F35, ECO:0007744|PDB:5F3D, ECO:0007744|PDB:5LQM, ECO:0007744|PDB:5LQS source Swiss-Prot : SWS_FT_FI2 28) chain A residue 254 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000269|PubMed:24650327, ECO:0000269|PubMed:27545412, ECO:0000269|PubMed:29641168, ECO:0007744|PDB:4P3X, ECO:0007744|PDB:5F33, ECO:0007744|PDB:5F35, ECO:0007744|PDB:5F3D, ECO:0007744|PDB:5LQM, ECO:0007744|PDB:5LQS source Swiss-Prot : SWS_FT_FI2 29) chain A residue 81 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000269|PubMed:24650327, ECO:0000269|PubMed:27545412, ECO:0000269|PubMed:29641168, ECO:0007744|PDB:4P3X, ECO:0007744|PDB:5F33, ECO:0007744|PDB:5F35, ECO:0007744|PDB:5F3D, ECO:0007744|PDB:5LQM, ECO:0007744|PDB:5LQS source Swiss-Prot : SWS_FT_FI2

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