eF-site ID 4wiu-A PDB Code 4wiu Chain A click to enlarge Title Crystal Structure of PEPCK (Rv0211) from Mycobacterium tuberculosis in complex with oxalate and Mn2+ Classification LYASE,TRANSFERASE Compound Phosphoenolpyruvate carboxykinase [GTP] Source Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) (PCKG_MYCTA) Sequence A:  SHMTSATIPGLDTAPTNHQGLLSWVEEVAELTQPDRVVFT DGSEEEFQRLCDQLVEAGTFIRLNPEKHKNSYLALSDPSD VARVESRTYICSAKEIDAGPTNNWMDPGEMRSIMKDLYRG CMRGRTMYVVPFCMGPLGAEDPKLGVEITDSEYVVVSMRT MTRMGKAALEKMGDDGFFVKALHSVGAPLEPGQKDVAWPC SETKYITHFPETREIWSYGSGYGGNALLGKKCYSLRIASA MAHDEGWLAEHMLILKLISPENKAYYFAAAFPSACGKTNL AMLQPTIPGWRAETLGDDIAWMRFGKDGRLYAVNPEFGFF GVAPGTNWKSNPNAMRTIAAGNTVFTNVALTDDGDVWWEG LEGDPQHLIDWKGNDWYFRETETNAAHPNSRYCTPMSQCP ILAPEWDDPQGVPISGILFGGRRKTTVPLVTEARDWQHGV FIGATLGSEQTNVRRDPMAMLPFLGYNVGDYFQHWINLGK HADESKLPKVFFVNWFRRGDDGRFLWPGFGENSRVLKWIV DRIEHKAGGATTPIGTVPAVEDLDLDGLDVDAADVAAALA VDADEWRQELPLIEEWLQFVGEKLPTGVKDEFDALKERLG Description Functional site 1) chain A residue 229 type sequence K description binding site for residue MN A 701 source : AC1 2) chain A residue 249 type sequence H description binding site for residue MN A 701 source : AC1 3) chain A residue 296 type sequence D description binding site for residue MN A 701 source : AC1 4) chain A residue 81 type sequence R description binding site for residue OXL A 702 source : AC2 5) chain A residue 229 type sequence K description binding site for residue OXL A 702 source : AC2 6) chain A residue 249 type sequence H description binding site for residue OXL A 702 source : AC2 7) chain A residue 389 type sequence R description binding site for residue OXL A 702 source : AC2 8) chain A residue 83 type sequence E description binding site for residue GOL A 703 source : AC3 9) chain A residue 86 type sequence T description binding site for residue GOL A 703 source : AC3 10) chain A residue 99 type sequence T description binding site for residue GOL A 703 source : AC3 11) chain A residue 100 type sequence N description binding site for residue GOL A 703 source : AC3 12) chain A residue 101 type sequence N description binding site for residue GOL A 703 source : AC3 13) chain A residue 234 type sequence R description binding site for residue GOL A 703 source : AC3 14) chain A residue 467 type sequence L description binding site for residue GOL A 703 source : AC3 15) chain A residue 468 type sequence P description binding site for residue GOL A 703 source : AC3 16) chain A residue 273 type ACT_SITE sequence C description ACT_SITE => ECO:0000250|UniProtKB:P07379, ECO:0000255|HAMAP-Rule:MF_00452 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 81 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000269|Ref.2 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 229 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000269|Ref.2 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 249 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000269|Ref.2 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 296 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000269|Ref.2 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 387 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000269|Ref.2 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 220 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P07379, ECO:0000255|HAMAP-Rule:MF_00452 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 271 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P07379, ECO:0000255|HAMAP-Rule:MF_00452 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 272 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P07379, ECO:0000255|HAMAP-Rule:MF_00452 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 389 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P07379, ECO:0000255|HAMAP-Rule:MF_00452 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 420 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P07379, ECO:0000255|HAMAP-Rule:MF_00452 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 515 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:P07379, ECO:0000255|HAMAP-Rule:MF_00452 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 269-277 type prosite sequence FPSACGKTN description PEPCK_GTP Phosphoenolpyruvate carboxykinase (GTP) signature. FPSACGKTN source prosite : PS00505

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