eF-site ID 6gmc-A PDB Code 6gmc Chain A click to enlarge Title 1.2 A resolution structure of human hydroxyacid oxidase 1 bound with FMN and 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1,2,3-thiadiazole Classification OXIDOREDUCTASE Compound Hydroxyacid oxidase 1 Source (HAOX1_HUMAN) Sequence A:  MLPRLICINDYEQHAKSVLPKSIYDYYRSGANDEETLADN IAAFSRWKLYPRMLRNVAETDLSTSVLGQRVSMPICVGAT AMQRMAHVDGELATVRACQSLGTGMMLSSWATSSIEEVAE AGPEALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVD TPYLGNRLDDVRNRFKLPPQLRMKNFSTLSFSPEENFGDD SGLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILRGD DAREAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAV EGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIVWGLA FQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVRK Description Functional site 1) chain A residue 52 type sequence R description binding site for residue EDO A 501 source : AC1 2) chain A residue 53 type sequence M description binding site for residue EDO A 501 source : AC1 3) chain A residue 54 type sequence L description binding site for residue EDO A 501 source : AC1 4) chain A residue 55 type sequence R description binding site for residue EDO A 501 source : AC1 5) chain A residue 159 type sequence V description binding site for residue EDO A 501 source : AC1 6) chain A residue 345 type sequence A description binding site for residue EDO A 501 source : AC1 7) chain A residue 348 type sequence G description binding site for residue EDO A 501 source : AC1 8) chain A residue 284 type sequence G description binding site for residue EDO A 502 source : AC2 9) chain A residue 285 type sequence K description binding site for residue EDO A 502 source : AC2 10) chain A residue 286 type sequence V description binding site for residue EDO A 502 source : AC2 11) chain A residue 287 type sequence E description binding site for residue EDO A 502 source : AC2 12) chain A residue 323 type sequence F description binding site for residue EDO A 502 source : AC2 13) chain A residue 324 type sequence Q description binding site for residue EDO A 502 source : AC2 14) chain A residue 327 type sequence K description binding site for residue EDO A 502 source : AC2 15) chain A residue 28 type sequence R description binding site for residue EDO A 503 source : AC3 16) chain A residue 37 type sequence L description binding site for residue EDO A 503 source : AC3 17) chain A residue 7 type sequence C description binding site for residue EDO A 504 source : AC4 18) chain A residue 32 type sequence N description binding site for residue EDO A 504 source : AC4 19) chain A residue 33 type sequence D description binding site for residue EDO A 504 source : AC4 20) chain A residue 168 type sequence L description binding site for residue EDO A 504 source : AC4 21) chain A residue 296 type sequence K description binding site for residue EDO A 504 source : AC4 22) chain A residue 339 type sequence E description binding site for residue EDO A 504 source : AC4 23) chain A residue 26 type sequence Y description binding site for residue FMN A 505 source : AC5 24) chain A residue 27 type sequence Y description binding site for residue FMN A 505 source : AC5 25) chain A residue 79 type sequence A description binding site for residue FMN A 505 source : AC5 26) chain A residue 80 type sequence T description binding site for residue FMN A 505 source : AC5 27) chain A residue 81 type sequence A description binding site for residue FMN A 505 source : AC5 28) chain A residue 108 type sequence S description binding site for residue FMN A 505 source : AC5 29) chain A residue 109 type sequence S description binding site for residue FMN A 505 source : AC5 30) chain A residue 110 type sequence W description binding site for residue FMN A 505 source : AC5 31) chain A residue 130 type sequence Q description binding site for residue FMN A 505 source : AC5 32) chain A residue 132 type sequence Y description binding site for residue FMN A 505 source : AC5 33) chain A residue 158 type sequence T description binding site for residue FMN A 505 source : AC5 34) chain A residue 236 type sequence K description binding site for residue FMN A 505 source : AC5 35) chain A residue 258 type sequence S description binding site for residue FMN A 505 source : AC5 36) chain A residue 260 type sequence H description binding site for residue FMN A 505 source : AC5 37) chain A residue 261 type sequence G description binding site for residue FMN A 505 source : AC5 38) chain A residue 263 type sequence R description binding site for residue FMN A 505 source : AC5 39) chain A residue 291 type sequence D description binding site for residue FMN A 505 source : AC5 40) chain A residue 292 type sequence G description binding site for residue FMN A 505 source : AC5 41) chain A residue 293 type sequence G description binding site for residue FMN A 505 source : AC5 42) chain A residue 295 type sequence R description binding site for residue FMN A 505 source : AC5 43) chain A residue 314 type sequence G description binding site for residue FMN A 505 source : AC5 44) chain A residue 315 type sequence R description binding site for residue FMN A 505 source : AC5 45) chain A residue 26 type sequence Y description binding site for residue C7C A 506 source : AC6 46) chain A residue 82 type sequence M description binding site for residue C7C A 506 source : AC6 47) chain A residue 110 type sequence W description binding site for residue C7C A 506 source : AC6 48) chain A residue 132 type sequence Y description binding site for residue C7C A 506 source : AC6 49) chain A residue 167 type sequence R description binding site for residue C7C A 506 source : AC6 50) chain A residue 183 type sequence M description binding site for residue C7C A 506 source : AC6 51) chain A residue 193 type sequence F description binding site for residue C7C A 506 source : AC6 52) chain A residue 205 type sequence L description binding site for residue C7C A 506 source : AC6 53) chain A residue 208 type sequence Y description binding site for residue C7C A 506 source : AC6 54) chain A residue 260 type sequence H description binding site for residue C7C A 506 source : AC6 55) chain A residue 263 type sequence R description binding site for residue C7C A 506 source : AC6 56) chain A residue 260 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00683 source Swiss-Prot : SWS_FT_FI1 57) chain A residue 184 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9WU19 source Swiss-Prot : SWS_FT_FI8 58) chain A residue 230 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI10 59) chain A residue 194 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9WU19 source Swiss-Prot : SWS_FT_FI9 60) chain A residue 26 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:18215067, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDU source Swiss-Prot : SWS_FT_FI2 61) chain A residue 132 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:18215067, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDU source Swiss-Prot : SWS_FT_FI2 62) chain A residue 260 type BINDING sequence H description BINDING => ECO:0000269|PubMed:18215067, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDU source Swiss-Prot : SWS_FT_FI2 63) chain A residue 263 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18215067, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDU source Swiss-Prot : SWS_FT_FI2 64) chain A residue 79 type BINDING sequence A description BINDING => ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U source Swiss-Prot : SWS_FT_FI3 65) chain A residue 108 type BINDING sequence S description BINDING => ECO:0000255|PROSITE-ProRule:PRU00683, ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U source Swiss-Prot : SWS_FT_FI4 66) chain A residue 158 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU00683, ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U source Swiss-Prot : SWS_FT_FI4 67) chain A residue 236 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00683, ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U source Swiss-Prot : SWS_FT_FI4 68) chain A residue 258-264 type prosite sequence SNHGARQ description FMN_HYDROXY_ACID_DH_1 FMN-dependent alpha-hydroxy acid dehydrogenases active site. SNHGARQ source prosite : PS00557 69) chain A residue 130 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU00683, ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2W0U source Swiss-Prot : SWS_FT_FI5 70) chain A residue 167 type BINDING sequence R description BINDING => ECO:0000269|PubMed:18215067, ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDU source Swiss-Prot : SWS_FT_FI6 71) chain A residue 258 type BINDING sequence S description BINDING => ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U source Swiss-Prot : SWS_FT_FI7 72) chain A residue 291 type BINDING sequence D description BINDING => ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U source Swiss-Prot : SWS_FT_FI7 73) chain A residue 314 type BINDING sequence G description BINDING => ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U source Swiss-Prot : SWS_FT_FI7

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