eF-site ID 1pj5-A PDB Code 1pj5 Chain A click to enlarge Title Crystal structure of dimethylglycine oxidase of Arthrobacter globiformis in complex with acetate Classification OXIDOREDUCTASE Compound N,N-dimethylglycine oxidase Source Arthrobacter globiformis (Q9AGP8_ARTGO) Sequence A:  TPRIVIIGAGIVGTNLADELVTRGWNNITVLDQGPLNMPG GSTSHAPGLVFQTNPSKTMASFAKYTVEKLLSLTEDGVSC FNQVGGLEVATTETRLADLKRKLGYAAAWGIEGRLLSPAE CQELYPLLDGENILGGLHVPSDGLASAARAVQLLIKRTES AGVTYRGSTTVTGIEQSGGRVTGVQTADGVIPADIVVSCA GFWGAKIGAMIGMAVPLLPLAHQYVKTTPVPAQQGRNDQP NGARLPILRHQDQDLYYREHGDRYGIGSYAHRPMPVDVDT LGAYAPETVSEHHMPSRLDFTLEDFLPAWEATKQLLPALA DSEIEDGFNGIFSFTPDGGPLLGESKELDGFYVAEAVWVT HSAGVAKAMAELLTTGRSETDLGECDITRFEDVQLTPEYV SETSQQNFVEIYDVLHPLQPRLSPRNLRVSPFHARHKELG AFFLEAGGWERPYWFEANAALLKEMPAEWLPPARDAWSGM FSSPIAAAEAWKTRTAVAMYDMTPLKRLEVSGPGALKLLQ ELTTADLAKKPGAVTYTLLLDHAGGVRSDITVARLSEDTF QLGANGNIDTAYFERAARHQTQSGSATDWVQVRDTTGGTC CIGLWGPLARDLVSKVSDDDFTNDGLKYFRAKNVVIGGIP VTAMRLSYVGELGWELYTSADNGQRLWDALWQAGQPFGVI AAGRAAFSSLRLEKGYRSWGTDMTTEHDPFEAGLGFAVKM AKESFIGKGALEGRTEEASARRLRCLTIDDGRSIVLGKEP VFYKEQAVGYVTSAAYGYTVAKPIAYSYLPGTVSVGDSVD IEYFGRRITATVTEDPLYDPKMTRLRG Description (1)  N,N-dimethylglycine oxidase, (E.C.1.5.3.10) Functional site 1) chain A residue 257 type sequence D description BINDING SITE FOR RESIDUE NA A 2001 source : AC1 2) chain A residue 412 type sequence V description BINDING SITE FOR RESIDUE NA A 2001 source : AC1 3) chain A residue 54 type sequence F description BINDING SITE FOR RESIDUE ACT A 2145 source : AC2 4) chain A residue 252 type sequence R description BINDING SITE FOR RESIDUE ACT A 2145 source : AC2 5) chain A residue 272 type sequence Y description BINDING SITE FOR RESIDUE ACT A 2145 source : AC2 6) chain A residue 361 type sequence W description BINDING SITE FOR RESIDUE ACT A 2145 source : AC2 7) chain A residue 415 type sequence Y description BINDING SITE FOR RESIDUE ACT A 2145 source : AC2 8) chain A residue 11 type sequence G description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 9) chain A residue 13 type sequence G description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 10) chain A residue 14 type sequence I description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 11) chain A residue 15 type sequence V description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 12) chain A residue 35 type sequence D description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 13) chain A residue 36 type sequence Q description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 14) chain A residue 42 type sequence P description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 15) chain A residue 44 type sequence G description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 16) chain A residue 45 type sequence S description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 17) chain A residue 46 type sequence T description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 18) chain A residue 48 type sequence H description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 19) chain A residue 49 type sequence A description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 20) chain A residue 50 type sequence P description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 21) chain A residue 51 type sequence G description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 22) chain A residue 52 type sequence L description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 23) chain A residue 172 type sequence T description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 24) chain A residue 173 type sequence T description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 25) chain A residue 174 type sequence V description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 26) chain A residue 202 type sequence C description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 27) chain A residue 203 type sequence A description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 28) chain A residue 204 type sequence G description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 29) chain A residue 206 type sequence W description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 30) chain A residue 210 type sequence I description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 31) chain A residue 225 type sequence H description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 32) chain A residue 259 type sequence Y description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 33) chain A residue 333 type sequence G description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 34) chain A residue 334 type sequence I description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 35) chain A residue 335 type sequence F description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 36) chain A residue 360 type sequence V description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 37) chain A residue 361 type sequence W description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 38) chain A residue 362 type sequence V description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 39) chain A residue 363 type sequence T description BINDING SITE FOR RESIDUE FAD A 902 source : AC3 40) chain A residue 225 type catalytic sequence H description 879 source MCSA : MCSA1 41) chain A residue 259 type catalytic sequence Y description 879 source MCSA : MCSA1 42) chain A residue 552 type catalytic sequence D description 879 source MCSA : MCSA1 43) chain A residue 225 type ACT_SITE sequence H description ACT_SITE => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 44) chain A residue 259 type ACT_SITE sequence Y description ACT_SITE => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 45) chain A residue 552 type ACT_SITE sequence D description For 5,10-methylenetetrahydrofolate synthesis activity => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 46) chain A residue 14 type BINDING sequence I description BINDING => ECO:0000269|PubMed:12912903, ECO:0000269|PubMed:19369258 source Swiss-Prot : SWS_FT_FI3 47) chain A residue 35 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12912903, ECO:0000269|PubMed:19369258 source Swiss-Prot : SWS_FT_FI3 48) chain A residue 45 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12912903, ECO:0000269|PubMed:19369258 source Swiss-Prot : SWS_FT_FI3 49) chain A residue 52 type BINDING sequence L description BINDING => ECO:0000269|PubMed:12912903, ECO:0000269|PubMed:19369258 source Swiss-Prot : SWS_FT_FI3 50) chain A residue 174 type BINDING sequence V description BINDING => ECO:0000269|PubMed:12912903, ECO:0000269|PubMed:19369258 source Swiss-Prot : SWS_FT_FI3 51) chain A residue 259 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:12912903, ECO:0000269|PubMed:19369258 source Swiss-Prot : SWS_FT_FI3 52) chain A residue 360 type BINDING sequence V description BINDING => ECO:0000269|PubMed:12912903, ECO:0000269|PubMed:19369258 source Swiss-Prot : SWS_FT_FI3 53) chain A residue 539 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:19369258 source Swiss-Prot : SWS_FT_FI4 54) chain A residue 554 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI5 55) chain A residue 566 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI5 56) chain A residue 658 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI5 57) chain A residue 552 type SITE sequence D description Important for catalytic activity => ECO:0000269|PubMed:19369258, ECO:0000305|PubMed:12912903 source Swiss-Prot : SWS_FT_FI7 58) chain A residue 225 type SITE sequence H description Important for catalytic activity => ECO:0000269|PubMed:12912903 source Swiss-Prot : SWS_FT_FI6 59) chain A residue 259 type SITE sequence Y description Important for catalytic activity => ECO:0000269|PubMed:12912903 source Swiss-Prot : SWS_FT_FI6 60) chain A residue 48 type MOD_RES sequence H description Pros-8alpha-FAD histidine source Swiss-Prot : SWS_FT_FI8

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