eF-site ID 1w6t-AB PDB Code 1w6t Chain A, B click to enlarge Title Crystal Structure Of Octameric Enolase From Streptococcus pneumoniae Classification LYASE Compound ENOLASE Source Streptococcus pneumoniae (strain ATCC BAA-255 / R6) (ENO_STRR6) Sequence A:  HMSIITDVYAREVLDSRGNPTLEVEVYTESGAFGRGMVPS GGEHEAVELRDGDKSRYGGLGTQKAVDNVNNIIAEAIIGY DVRDQQAIDRAMIALDGTPNKGKLGANAILGVSIAVARAA ADYLEIPLYSYLGGFNTKVLPTPMMNIINGGSHSDAPIAF QEFMILPVGAPTFKEALRYGAEIFHALKKILKSRGLETAV GDEGGFAPRFEGTEDGVETILAAIEAAGYVPGKDVFLGFD CASSEFYDRKVYDYTKFEGEGAAVRTSAEQIDYLEELVNK YPIITIEDGMDENDWDGWKALTERLGKKVQLVGDDFFVTN TDYLARGIQEGAANSILIKVNQIGTLTETFEAIEMAKEAG YTAVVSHRSGETEDSTIADIAVATNAGQIKTGSLSRTDRI AKYNQLLRIEDQLGEVAEYRGLKSFYNLK B:  HMSIITDVYAREVLDSRGNPTLEVEVYTESGAFGRGMVPS GGEHEAVELRDGDKSRYGGLGTQKAVDNVNNIIAEAIIGY DVRDQQAIDRAMIALDGTPNKGKLGANAILGVSIAVARAA ADYLEIPLYSYLGGFNTKVLPTPMMNIINGGSHSDAPIAF QEFMILPVGAPTFKEALRYGAEIFHALKKILKSRGLETAV GDEGGFAPRFEGTEDGVETILAAIEAAGYVPGKDVFLGFD CASSEFYDKERKVYDYTKFEGEGAAVRTSAEQIDYLEELV NKYPIITIEDGMDENDWDGWKALTERLGKKVQLVGDDFFV TNTDYLARGIQEGAANSILIKVNQIGTLTETFEAIEMAKE AGYTAVVSHRSGETEDSTIADIAVATNAGQIKTGSLSRTD RIAKYNQLLRIEDQLGEVAEYRGLKSFYNLK Description Functional site 1) chain A residue 242 type sequence D description BINDING SITE FOR RESIDUE MG A 435 source : AC1 2) chain A residue 291 type sequence E description BINDING SITE FOR RESIDUE MG A 435 source : AC1 3) chain A residue 318 type sequence D description BINDING SITE FOR RESIDUE MG A 435 source : AC1 4) chain B residue 242 type sequence D description BINDING SITE FOR RESIDUE MG B 435 source : AC2 5) chain B residue 291 type sequence E description BINDING SITE FOR RESIDUE MG B 435 source : AC2 6) chain B residue 318 type sequence D description BINDING SITE FOR RESIDUE MG B 435 source : AC2 7) chain A residue 77 type sequence E description BINDING SITE FOR RESIDUE 2PE A1434 source : AC3 8) chain A residue 78 type sequence A description BINDING SITE FOR RESIDUE 2PE A1434 source : AC3 9) chain A residue 80 type sequence I description BINDING SITE FOR RESIDUE 2PE A1434 source : AC3 10) chain B residue 77 type sequence E description BINDING SITE FOR RESIDUE 2PE B1434 source : AC4 11) chain B residue 78 type sequence A description BINDING SITE FOR RESIDUE 2PE B1434 source : AC4 12) chain B residue 80 type sequence I description BINDING SITE FOR RESIDUE 2PE B1434 source : AC4 13) chain B residue 81 type sequence G description BINDING SITE FOR RESIDUE 2PE B1434 source : AC4 14) chain B residue 82 type sequence Y description BINDING SITE FOR RESIDUE 2PE B1434 source : AC4 15) chain A residue 205 type ACT_SITE sequence E description Proton donor => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI1 16) chain B residue 205 type ACT_SITE sequence E description Proton donor => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 343 type ACT_SITE sequence K description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 343 type ACT_SITE sequence K description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 155 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 20) chain B residue 242 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 21) chain B residue 291 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 22) chain B residue 318 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 23) chain B residue 370 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 24) chain B residue 394 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 164 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 242 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 291 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 318 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 29) chain A residue 370 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 394 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 31) chain B residue 155 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 32) chain B residue 164 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 340-353 type prosite sequence ILIKVNQIGTLTET description ENOLASE Enolase signature. ILIKvNQIGTLTET source prosite : PS00164 34) chain A residue 343 type BINDING sequence K description covalent; in inhibited form => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI4 35) chain B residue 343 type BINDING sequence K description covalent; in inhibited form => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI4

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