eF-site ID 2dwc-B PDB Code 2dwc Chain B click to enlarge Title Crystal structure of Probable phosphoribosylglycinamide formyl transferase from Pyrococcus horikoshii OT3 complexed with ADP Classification TRANSFERASE Compound 433aa long hypothetical phosphoribosylglycinamide formyl transferase Source null (O58056_PYRHO) Sequence B:  VVMIKLRDELGTATTDSAQKILLLGSGELGKEIAIEAQRL GVEVVAVDRYANAPAMQVAHRSYVGNMMDKDFLWSVVERE KPDAIIPEIEAINLDALFEFEKDGYFVVPNARATWIAMHR ERLRETLVKEAKVPTSRYMYATTLDELYEACEKIGYPCHT KAIMSGSYFVKGPEDIPKAWEEEKIIVEEHIDFDVEVTEL AVRHFDENGEIVTTFPKPVGHYQIDGDYHASWQPAEISEK AEREVYRIAKRITDVLGGLGIFGVEMFVKGDKVWANEVSP RPHDTGMVTLASHPPGFSEFALHLRAVLGLPIPGEWVDGY RLFPMLIPAATHVIKAKVSGYSPRFRGLVKALSVPNATVR LFGKPEAYVGRRLGIALAWDKDVEVAKRKAEMVAHMIELR TRSSDWHDQ Description Functional site 1) chain B residue 378 type sequence K description BINDING SITE FOR RESIDUE SO4 B 601 source : AC1 2) chain B residue 382 type sequence Y description BINDING SITE FOR RESIDUE SO4 B 601 source : AC1 3) chain B residue 385 type sequence R description BINDING SITE FOR RESIDUE SO4 B 601 source : AC1 4) chain B residue 414 type sequence R description BINDING SITE FOR RESIDUE SO4 B 603 source : AC3 5) chain B residue 420 type sequence W description BINDING SITE FOR RESIDUE SO4 B 603 source : AC3 6) chain B residue 121 type sequence R description BINDING SITE FOR RESIDUE ADP B 502 source : AC6 7) chain B residue 160 type sequence H description BINDING SITE FOR RESIDUE ADP B 502 source : AC6 8) chain B residue 162 type sequence K description BINDING SITE FOR RESIDUE ADP B 502 source : AC6 9) chain B residue 202 type sequence E description BINDING SITE FOR RESIDUE ADP B 502 source : AC6 10) chain B residue 203 type sequence E description BINDING SITE FOR RESIDUE ADP B 502 source : AC6 11) chain B residue 204 type sequence H description BINDING SITE FOR RESIDUE ADP B 502 source : AC6 12) chain B residue 205 type sequence I description BINDING SITE FOR RESIDUE ADP B 502 source : AC6 13) chain B residue 207 type sequence F description BINDING SITE FOR RESIDUE ADP B 502 source : AC6 14) chain B residue 210 type sequence E description BINDING SITE FOR RESIDUE ADP B 502 source : AC6 15) chain B residue 237 type sequence Q description BINDING SITE FOR RESIDUE ADP B 502 source : AC6 16) chain B residue 281 type sequence F description BINDING SITE FOR RESIDUE ADP B 502 source : AC6 17) chain B residue 290 type sequence N description BINDING SITE FOR RESIDUE ADP B 502 source : AC6 18) chain B residue 291 type sequence E description BINDING SITE FOR RESIDUE ADP B 502 source : AC6 19) chain B residue 279 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_01643 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 291 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_01643 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 298 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01643 source Swiss-Prot : SWS_FT_FI1 22) chain B residue 378 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_01643 source Swiss-Prot : SWS_FT_FI1 23) chain B residue 385 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01643 source Swiss-Prot : SWS_FT_FI1 24) chain B residue 29 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_01643 source Swiss-Prot : SWS_FT_FI1 25) chain B residue 89 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_01643 source Swiss-Prot : SWS_FT_FI1 26) chain B residue 121 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01643, ECO:0000269|Ref.3 source Swiss-Prot : SWS_FT_FI2 27) chain B residue 162 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_01643, ECO:0000269|Ref.3 source Swiss-Prot : SWS_FT_FI2 28) chain B residue 202 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_01643, ECO:0000269|Ref.3 source Swiss-Prot : SWS_FT_FI2 29) chain B residue 210 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_01643, ECO:0000269|Ref.3 source Swiss-Prot : SWS_FT_FI2

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