eF-site ID 1a0e-A PDB Code 1a0e Chain A Title XYLOSE ISOMERASE FROM THERMOTOGA NEAPOLITANA Classification KETOLISOMERASE Compound XYLOSE ISOMERASE Source null (XYLA_THENE) Sequence A:  AEFFPEIPKVQFEGKESTNPLAFKFYDPEEIIDGKPLKDH LKFSVAFWHTFVNEGRDPFGDPTADRPWNRYTDPMDKAFA RVDALFEFCEKLNIEYFCFHDRDIAPEGKTLRETNKILDK VVERIKERMKDSNVKLLWGTANLFSHPRYMHGAATTCSAD VFAYAAAQVKKALEITKELGGEGYVFWGGREGYETLLNTD LGFELENLARFLRMAVDYAKRIGFTGQFLIEPKPKEPTKH QYDFDVATAYAFLKSHGLDEYFKFNIEANHATLAGHTFQH ELRMARILGKLGSIDANQGDLLLGWDTDQFPTNVYDTTLA MYEVIKAGGFTKGGLNFDAKVRRASYKVEDLFIGHIAGMD TFALGFKVAYKLVKDGVLDKFIEEKYRSFREGIGRDIVEG KVDFEKLEEYIIDKETIELPSGKQEYLESLINSYIVKTIL ELR Description Functional site 1) chain A residue 231 type sequence E description CO BINDING SITE 1 OF MOLECULE A source : CO1 2) chain A residue 267 type sequence E description CO BINDING SITE 1 OF MOLECULE A source : CO1 3) chain A residue 295 type sequence D description CO BINDING SITE 1 OF MOLECULE A source : CO1 4) chain A residue 338 type sequence D description CO BINDING SITE 1 OF MOLECULE A source : CO1 5) chain A residue 267 type sequence E description CO BINDING SITE 2 OF MOLECULE A (HOH629 WAS ADDED AFTER LAST REFINEMENT RESULTED IN A NEW FO-FC PEAK AT THIS SITE). source : CO2 6) chain A residue 270 type sequence H description CO BINDING SITE 2 OF MOLECULE A (HOH629 WAS ADDED AFTER LAST REFINEMENT RESULTED IN A NEW FO-FC PEAK AT THIS SITE). source : CO2 7) chain A residue 2 type sequence E description CO BINDING SITE 3 OF MOLECULE A (SITE CO3 IS ON A CRYSTALLOGRAPHIC TWO-FOLD SYMMETRY AXIS: INTERPRETATION OF THE OBSERVED DENSITY PEAK AS A CO CATION WAS PRAGMATIC RATHER THAN RIGOROUS, AS THIS SITE IS CLEARLY NOT A FEATURE OF THE PROTEIN IN SOLUTION). source : CO3 8) chain A residue 231 type sequence E description BINDING SITE FOR RESIDUE CO A 491 source : AC1 9) chain A residue 267 type sequence E description BINDING SITE FOR RESIDUE CO A 491 source : AC1 10) chain A residue 295 type sequence D description BINDING SITE FOR RESIDUE CO A 491 source : AC1 11) chain A residue 338 type sequence D description BINDING SITE FOR RESIDUE CO A 491 source : AC1 12) chain A residue 267 type sequence E description BINDING SITE FOR RESIDUE CO A 492 source : AC2 13) chain A residue 270 type sequence H description BINDING SITE FOR RESIDUE CO A 492 source : AC2 14) chain A residue 306 type sequence D description BINDING SITE FOR RESIDUE CO A 492 source : AC2 15) chain A residue 308 type sequence D description BINDING SITE FOR RESIDUE CO A 492 source : AC2 16) chain A residue 2 type sequence E description BINDING SITE FOR RESIDUE CO A 493 source : AC3 17) chain A residue 2 type sequence E description BINDING SITE FOR RESIDUE CO A 493 source : AC3 18) chain A residue 100 type ACT_SITE sequence H description source Swiss-Prot : SWS_FT_FI1 19) chain A residue 103 type ACT_SITE sequence D description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 231 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 21) chain A residue 267 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 22) chain A residue 270 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 23) chain A residue 295 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 24) chain A residue 306 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 25) chain A residue 308 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 26) chain A residue 338 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3

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