eF-site ID 6c4j-L PDB Code 6c4j Chain L click to enlarge Title Ligand bound full length hUGDH with A104L substitution Classification OXIDOREDUCTASE Compound UDP-glucose 6-dehydrogenase Source (UGDH_HUMAN) Sequence L:  MFEIKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNES RINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIK EADLVFISVNTPTKTYGMGKGRALDLKYIEACARRIVQNS NGYKIVTEKSTVPVRAAESIRRIFDANTKPNLNLQVLSNP EFLAEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYE HWVPREKILTTNTWSSELSKLAANAFLAQRISSINSISAL CEATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKD VLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIID SLFNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDE GAHLHIYDPKVPREQIVVDLSHDQVSRLVTISKDPYEACD GAHAVVICTEWDMFKELDYERIHKKMLKPAFIFDGRRVLD GLHNELQTIGFQIETIGKKV Description Functional site 1) chain L residue 260 type sequence R description binding site for residue UPG K 502 source : AG6 2) chain L residue 260 type sequence R description binding site for residue PGO K 506 source : AH1 3) chain L residue 10 type sequence I description binding site for residue NAD L 501 source : AH2 4) chain L residue 11 type sequence G description binding site for residue NAD L 501 source : AH2 5) chain L residue 13 type sequence G description binding site for residue NAD L 501 source : AH2 6) chain L residue 14 type sequence Y description binding site for residue NAD L 501 source : AH2 7) chain L residue 15 type sequence V description binding site for residue NAD L 501 source : AH2 8) chain L residue 36 type sequence D description binding site for residue NAD L 501 source : AH2 9) chain L residue 41 type sequence R description binding site for residue NAD L 501 source : AH2 10) chain L residue 88 type sequence S description binding site for residue NAD L 501 source : AH2 11) chain L residue 89 type sequence V description binding site for residue NAD L 501 source : AH2 12) chain L residue 91 type sequence T description binding site for residue NAD L 501 source : AH2 13) chain L residue 108 type sequence Y description binding site for residue NAD L 501 source : AH2 14) chain L residue 130 type sequence S description binding site for residue NAD L 501 source : AH2 15) chain L residue 131 type sequence T description binding site for residue NAD L 501 source : AH2 16) chain L residue 161 type sequence E description binding site for residue NAD L 501 source : AH2 17) chain L residue 279 type sequence K description binding site for residue NAD L 501 source : AH2 18) chain L residue 162 type sequence F description binding site for residue UPG L 502 source : AH3 19) chain L residue 163 type sequence L description binding site for residue UPG L 502 source : AH3 20) chain L residue 164 type sequence A description binding site for residue UPG L 502 source : AH3 21) chain L residue 165 type sequence E description binding site for residue UPG L 502 source : AH3 22) chain L residue 220 type sequence K description binding site for residue UPG L 502 source : AH3 23) chain L residue 224 type sequence N description binding site for residue UPG L 502 source : AH3 24) chain L residue 231 type sequence I description binding site for residue UPG L 502 source : AH3 25) chain L residue 265 type sequence F description binding site for residue UPG L 502 source : AH3 26) chain L residue 266 type sequence L description binding site for residue UPG L 502 source : AH3 27) chain L residue 267 type sequence K description binding site for residue UPG L 502 source : AH3 28) chain L residue 269 type sequence S description binding site for residue UPG L 502 source : AH3 29) chain L residue 272 type sequence F description binding site for residue UPG L 502 source : AH3 30) chain L residue 273 type sequence G description binding site for residue UPG L 502 source : AH3 31) chain L residue 276 type sequence C description binding site for residue UPG L 502 source : AH3 32) chain L residue 277 type sequence F description binding site for residue UPG L 502 source : AH3 33) chain L residue 338 type sequence F description binding site for residue UPG L 502 source : AH3 34) chain L residue 339 type sequence K description binding site for residue UPG L 502 source : AH3 35) chain L residue 442 type sequence R description binding site for residue UPG L 502 source : AH3 36) chain L residue 135 type sequence R description binding site for residue CL L 503 source : AH4 37) chain L residue 99 type sequence G description binding site for residue CL L 504 source : AH5 38) chain L residue 162 type sequence F description binding site for residue PGO L 505 source : AH6 39) chain L residue 171 type sequence D description binding site for residue PGO L 505 source : AH6 40) chain L residue 176 type sequence D description binding site for residue PGO L 505 source : AH6 41) chain L residue 161 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000269|PubMed:22123821 source Swiss-Prot : SWS_FT_FI1 42) chain L residue 220 type ACT_SITE sequence K description Proton donor/acceptor => ECO:0000269|PubMed:22123821 source Swiss-Prot : SWS_FT_FI1 43) chain L residue 276 type ACT_SITE sequence C description Nucleophile => ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21984906, ECO:0000269|PubMed:22123821 source Swiss-Prot : SWS_FT_FI2 44) chain L residue 11 type BINDING sequence G description BINDING => ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21595445, ECO:0000269|PubMed:21984906, ECO:0007744|PDB:2Q3E, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:3TDK source Swiss-Prot : SWS_FT_FI3 45) chain L residue 36 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21595445, ECO:0000269|PubMed:21984906, ECO:0007744|PDB:2Q3E, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:3TDK source Swiss-Prot : SWS_FT_FI3 46) chain L residue 41 type BINDING sequence R description BINDING => ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21595445, ECO:0000269|PubMed:21984906, ECO:0007744|PDB:2Q3E, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:3TDK source Swiss-Prot : SWS_FT_FI3 47) chain L residue 89 type BINDING sequence V description BINDING => ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21595445, ECO:0000269|PubMed:21984906, ECO:0007744|PDB:2Q3E, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:3TDK source Swiss-Prot : SWS_FT_FI3 48) chain L residue 276 type BINDING sequence C description BINDING => ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21595445, ECO:0000269|PubMed:21984906, ECO:0007744|PDB:2Q3E, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:3TDK source Swiss-Prot : SWS_FT_FI3 49) chain L residue 130 type BINDING sequence S description BINDING => ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21595445 source Swiss-Prot : SWS_FT_FI4 50) chain L residue 161 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23106432, ECO:0000305|PubMed:21502315, ECO:0000305|PubMed:21595445, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:4EDF source Swiss-Prot : SWS_FT_FI5 51) chain L residue 220 type BINDING sequence K description BINDING => ECO:0000269|PubMed:23106432, ECO:0000305|PubMed:21502315, ECO:0000305|PubMed:21595445, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:4EDF source Swiss-Prot : SWS_FT_FI5 52) chain L residue 267 type BINDING sequence K description BINDING => ECO:0000269|PubMed:23106432, ECO:0000305|PubMed:21502315, ECO:0000305|PubMed:21595445, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:4EDF source Swiss-Prot : SWS_FT_FI5 53) chain L residue 338 type BINDING sequence F description BINDING => ECO:0000269|PubMed:23106432, ECO:0000305|PubMed:21502315, ECO:0000305|PubMed:21595445, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:4EDF source Swiss-Prot : SWS_FT_FI5 54) chain L residue 165 type BINDING sequence E description BINDING => ECO:0000269|PubMed:21502315, ECO:0007744|PDB:2Q3E, ECO:0007744|PDB:2QG4 source Swiss-Prot : SWS_FT_FI6 55) chain L residue 107 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI10 56) chain L residue 260 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23106432, ECO:0000269|PubMed:27966912, ECO:0000305|PubMed:21502315, ECO:0000305|PubMed:21595445, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:4EDF, ECO:0007744|PDB:5TJH source Swiss-Prot : SWS_FT_FI7 57) chain L residue 346 type BINDING sequence R description BINDING => ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21595445, ECO:0000269|PubMed:21984906, ECO:0000269|PubMed:22123821, ECO:0007744|PDB:2Q3E, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:3TDK source Swiss-Prot : SWS_FT_FI8 58) chain L residue 442 type BINDING sequence R description BINDING => ECO:0000269|PubMed:22123821, ECO:0000269|PubMed:23106432, ECO:0000305|PubMed:21502315, ECO:0000305|PubMed:21595445, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3KHU, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:4EDF source Swiss-Prot : SWS_FT_FI9

Display surface Download Links