eF-site ID 6f9g-ABCDE PDB Code 6f9g Chain A, B, C, D, E click to enlarge Title Ligand binding domain of P. putida KT2440 polyamine chemorecpetors McpU in complex putrescine. Classification SIGNALING PROTEIN Compound Methyl-accepting chemotaxis protein McpU Source (MCPU_PSEPK) Sequence A:  SARQRLQAHAETQALRIQRYFMDAYQYGNGFARLVQVLKD RGGSDLRAELTRQARASLAGNPDVIGLYLVFQPNALDQQD SHYLGQDAMGSNESGRFSLYWSQPSPGTLELEAMPETMLG DTSIGSNGAAKNRWLTCPQDTARTCMLEPYLDEVNGRQVL MTSIALPLLEHGKVVGVVGLDIGLANLQQLSVNGRRDLFD GQGQVSIATAAGLLAGNSRDDSVLGKPMDKSVADGLLRVA HPFTPIPDTAPWQVVLELPES B:  SARQRLQAHAETQALRIQRYFMDAYQYGNGFARLVQVLKD RGGSDLRAELTRQARASLAGNPDVIGLYLVFQPNALDQQD SHYLGQDAMGSNESGRFSLYWSQPSPGTLELEAMPETMLG DTSIGSNGAAKNRWLTCPQDTARTCMLEPYLDEVNGRQVL MTSIALPLLEHGKVVGVVGLDIGLANLQQLSVNGRRDLFD GQGQVSIATAAGLLAGNSRDDSVLGKPMDKSVADGLLRVA HPFTPIPDTAPWQVVLELPES C:  ARQRLQAHAETQALRIQRYFMDAYQYGNGFARLVQVLKDR GGSDLRAELTRQARASLAGNPDVIGLYLVFQPNALDQQDS HYLGQDAMGSNESGRFSLYWSQPSPGTLELEAMPETMLGD TSIGSNGAAKNRWLTCPQDTARTCMLEPYLDEVNGRQVLM TSIALPLLEHGKVVGVVGLDIGLANLQQLSVNGRRDLFDG QGQVSIATAAGLLAGNSRDDSVLGKPMDKSVADGLLRVAH PFTPIPDTAPWQVVLELPES D:  DSARQRLQAHAETQALRIQRYFMDAYQYGNGFARLVQVLK DRGGSDLRAELTRQARASLAGNPDVIGLYLVFQPNALDQQ DSHYLGQDAMGSNESGRFSLYWSQPSPGTLELEAMPETML GDTSIGSNGAAKNRWLTCPQDTARTCMLEPYLDEVNGRQV LMTSIALPLLEHGKVVGVVGLDIGLANLQQLSVNGRRDLF DGQGQVSIATAAGLLAGNSRDDSVLGKPMDKSVADGLLRV AHPFTPIPDTAPWQVVLELPES E:  SARQRLQAHAETQALRIQRYFMDAYQYGNGFARLVQVLKD RGGSDLRAELTRQARASLAGNPDVIGLYLVFQPNALDQQD SHYLGQDAMGSNESGRFSLYWSQPSPGTLELEAMPETMLG DTSIGSNGAAKNRWLTCPQDTARTCMLEPYLDEVNGRQVL MTSIALPLLEHGKVVGVVGLDIGLANLQQLSVNGRRDLFD GQGQVSIATAAGLLAGNSRDDSVLGKPMDKSVADGLLRVA HPFTPIPDTAPWQVVLELPES Description (1)  Methyl-accepting chemotaxis protein PctB Functional site 1) chain A residue 120 type sequence Y description binding site for residue PUT A 401 source : AC1 2) chain A residue 170 type sequence M description binding site for residue PUT A 401 source : AC1 3) chain A residue 186 type sequence W description binding site for residue PUT A 401 source : AC1 4) chain A residue 202 type sequence Y description binding site for residue PUT A 401 source : AC1 5) chain A residue 204 type sequence D description binding site for residue PUT A 401 source : AC1 6) chain A residue 205 type sequence E description binding site for residue PUT A 401 source : AC1 7) chain A residue 213 type sequence M description binding site for residue PUT A 401 source : AC1 8) chain A residue 233 type sequence D description binding site for residue PUT A 401 source : AC1 9) chain A residue 300 type sequence D description binding site for residue GOL A 402 source : AC2 10) chain A residue 302 type sequence A description binding site for residue GOL A 402 source : AC2 11) chain B residue 120 type sequence Y description binding site for residue PUT B 401 source : AC3 12) chain B residue 152 type sequence Y description binding site for residue PUT B 401 source : AC3 13) chain B residue 166 type sequence M description binding site for residue PUT B 401 source : AC3 14) chain B residue 170 type sequence M description binding site for residue PUT B 401 source : AC3 15) chain B residue 186 type sequence W description binding site for residue PUT B 401 source : AC3 16) chain B residue 202 type sequence Y description binding site for residue PUT B 401 source : AC3 17) chain B residue 204 type sequence D description binding site for residue PUT B 401 source : AC3 18) chain B residue 213 type sequence M description binding site for residue PUT B 401 source : AC3 19) chain B residue 233 type sequence D description binding site for residue PUT B 401 source : AC3 20) chain C residue 152 type sequence Y description binding site for residue PUT C 401 source : AC4 21) chain C residue 166 type sequence M description binding site for residue PUT C 401 source : AC4 22) chain C residue 170 type sequence M description binding site for residue PUT C 401 source : AC4 23) chain C residue 186 type sequence W description binding site for residue PUT C 401 source : AC4 24) chain C residue 202 type sequence Y description binding site for residue PUT C 401 source : AC4 25) chain C residue 204 type sequence D description binding site for residue PUT C 401 source : AC4 26) chain C residue 205 type sequence E description binding site for residue PUT C 401 source : AC4 27) chain C residue 213 type sequence M description binding site for residue PUT C 401 source : AC4 28) chain C residue 233 type sequence D description binding site for residue PUT C 401 source : AC4 29) chain C residue 171 type sequence L description binding site for residue ACT C 402 source : AC5 30) chain C residue 191 type sequence Q description binding site for residue ACT C 402 source : AC5 31) chain D residue 120 type sequence Y description binding site for residue PUT D 401 source : AC6 32) chain D residue 166 type sequence M description binding site for residue PUT D 401 source : AC6 33) chain D residue 186 type sequence W description binding site for residue PUT D 401 source : AC6 34) chain D residue 202 type sequence Y description binding site for residue PUT D 401 source : AC6 35) chain D residue 204 type sequence D description binding site for residue PUT D 401 source : AC6 36) chain D residue 205 type sequence E description binding site for residue PUT D 401 source : AC6 37) chain D residue 233 type sequence D description binding site for residue PUT D 401 source : AC6 38) chain D residue 124 type sequence Q description binding site for residue ACT D 402 source : AC7 39) chain D residue 148 type sequence R description binding site for residue ACT D 402 source : AC7 40) chain D residue 171 type sequence L description binding site for residue ACT D 402 source : AC7 41) chain D residue 188 type sequence T description binding site for residue ACT D 402 source : AC7 42) chain D residue 191 type sequence Q description binding site for residue ACT D 402 source : AC7 43) chain D residue 107 type sequence R description binding site for residue GOL D 403 source : AC8 44) chain E residue 300 type sequence D description binding site for residue GOL D 403 source : AC8 45) chain E residue 302 type sequence A description binding site for residue GOL D 403 source : AC8 46) chain D residue 114 type sequence P description binding site for residue GOL D 404 source : AC9 47) chain D residue 115 type sequence D description binding site for residue GOL D 404 source : AC9 48) chain E residue 120 type sequence Y description binding site for residue PUT E 401 source : AD1 49) chain E residue 152 type sequence Y description binding site for residue PUT E 401 source : AD1 50) chain E residue 166 type sequence M description binding site for residue PUT E 401 source : AD1 51) chain E residue 170 type sequence M description binding site for residue PUT E 401 source : AD1 52) chain E residue 186 type sequence W description binding site for residue PUT E 401 source : AD1 53) chain E residue 202 type sequence Y description binding site for residue PUT E 401 source : AD1 54) chain E residue 204 type sequence D description binding site for residue PUT E 401 source : AD1 55) chain E residue 205 type sequence E description binding site for residue PUT E 401 source : AD1 56) chain E residue 213 type sequence M description binding site for residue PUT E 401 source : AD1 57) chain E residue 233 type sequence D description binding site for residue PUT E 401 source : AD1 58) chain C residue 302 type sequence A description binding site for residue GOL E 402 source : AD2 59) chain C residue 303 type sequence P description binding site for residue GOL E 402 source : AD2 60) chain E residue 163 type sequence L description binding site for residue GOL E 402 source : AD2 61) chain E residue 85 type sequence R description binding site for residue GOL E 403 source : AD3 62) chain E residue 233 type BINDING sequence D description BINDING => ECO:0000269|PubMed:29758259, ECO:0007744|PDB:6F9G source Swiss-Prot : SWS_FT_FI1 63) chain C residue 233 type BINDING sequence D description BINDING => ECO:0000269|PubMed:29758259, ECO:0007744|PDB:6F9G source Swiss-Prot : SWS_FT_FI1 64) chain D residue 202 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:29758259, ECO:0007744|PDB:6F9G source Swiss-Prot : SWS_FT_FI1 65) chain D residue 233 type BINDING sequence D description BINDING => ECO:0000269|PubMed:29758259, ECO:0007744|PDB:6F9G source Swiss-Prot : SWS_FT_FI1 66) chain E residue 202 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:29758259, ECO:0007744|PDB:6F9G source Swiss-Prot : SWS_FT_FI1 67) chain A residue 202 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:29758259, ECO:0007744|PDB:6F9G source Swiss-Prot : SWS_FT_FI1 68) chain A residue 233 type BINDING sequence D description BINDING => ECO:0000269|PubMed:29758259, ECO:0007744|PDB:6F9G source Swiss-Prot : SWS_FT_FI1 69) chain B residue 202 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:29758259, ECO:0007744|PDB:6F9G source Swiss-Prot : SWS_FT_FI1 70) chain B residue 233 type BINDING sequence D description BINDING => ECO:0000269|PubMed:29758259, ECO:0007744|PDB:6F9G source Swiss-Prot : SWS_FT_FI1 71) chain C residue 202 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:29758259, ECO:0007744|PDB:6F9G source Swiss-Prot : SWS_FT_FI1

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