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3MYY

Structure of E. Coli CheY mutant A113P bound to Beryllium fluoride

Functional Information from GO Data
ChainGOidnamespacecontents
A0000156molecular_functionphosphorelay response regulator activity
A0000160biological_processphosphorelay signal transduction system
A0000287molecular_functionmagnesium ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006935biological_processchemotaxis
A0007165biological_processsignal transduction
A0009288cellular_componentbacterial-type flagellum
A0009433cellular_componentbacterial-type flagellum basal body, C ring
A0009454biological_processaerotaxis
A0016407molecular_functionacetyltransferase activity
A0018393biological_processinternal peptidyl-lysine acetylation
A0043052biological_processthermotaxis
A0046872molecular_functionmetal ion binding
A0050920biological_processregulation of chemotaxis
A0071977biological_processbacterial-type flagellum-dependent swimming motility
A0097588biological_processarchaeal or bacterial-type flagellum-dependent cell motility
A0120107cellular_componentbacterial-type flagellum rotor complex
A1902021biological_processregulation of bacterial-type flagellum-dependent cell motility
B0000156molecular_functionphosphorelay response regulator activity
B0000160biological_processphosphorelay signal transduction system
B0000287molecular_functionmagnesium ion binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006935biological_processchemotaxis
B0007165biological_processsignal transduction
B0009288cellular_componentbacterial-type flagellum
B0009433cellular_componentbacterial-type flagellum basal body, C ring
B0009454biological_processaerotaxis
B0016407molecular_functionacetyltransferase activity
B0018393biological_processinternal peptidyl-lysine acetylation
B0043052biological_processthermotaxis
B0046872molecular_functionmetal ion binding
B0050920biological_processregulation of chemotaxis
B0071977biological_processbacterial-type flagellum-dependent swimming motility
B0097588biological_processarchaeal or bacterial-type flagellum-dependent cell motility
B0120107cellular_componentbacterial-type flagellum rotor complex
B1902021biological_processregulation of bacterial-type flagellum-dependent cell motility
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BEF A 130
ChainResidue
AASP57
ATRP58
AASN59
ATHR87
AALA88
ALYS109
AMN131
AHOH243
AHOH252

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 131
ChainResidue
AASP13
AASP57
AASN59
ABEF130
AHOH139
AHOH174

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 501
ChainResidue
AARG19
ALYS70
AHOH175
AHOH197
AHOH207
AHOH323
AHOH390
BLYS126
BHOH333

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 503
ChainResidue
ATRP58
AASN59
AGLU89
AASN94
AHOH165
AHOH311
AHOH370

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 504
ChainResidue
ALYS7
AASN32
AGLY50
AHOH374
AHOH379
AHOH387

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 505
ChainResidue
ALYS91
ALYS92
AGLU93
BHOH168

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BEF A 132
ChainResidue
AGLU35
AASP41
ALYS45
AHOH247
AHOH270
AHOH290

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN A 133
ChainResidue
ASER15
AHOH386

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN A 134
ChainResidue
AGLY50

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 135
ChainResidue
ALYS92
AHOH229
AHOH241
AHOH376
BLYS91
BLYS92

site_idBC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BEF B 130
ChainResidue
BASP57
BTRP58
BASN59
BTHR87
BALA88
BLYS109
BMN131
BHOH153
BHOH241

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 131
ChainResidue
BASP13
BASP57
BASN59
BBEF130
BHOH137
BHOH142

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 502
ChainResidue
BTRP58
BGLU89
BHOH292

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 506
ChainResidue
BLYS7
BASN32
BGLY50
BHOH192

site_idBC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 507
ChainResidue
BLEU46
BGLY49
BGLY50
BTYR51
BALA77
BMET78
BSO4134
BHOH348

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BEF B 1
ChainResidue
BGLU35
BASP41
BHOH285
BHOH343
BHOH360

site_idBC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MN B 132
ChainResidue
BHOH162
ALYS119
AHOH168
AHOH220
AHOH241
AHOH245
AHOH308
BLYS92
BGLU93

site_idBC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN B 133
ChainResidue
BSER15

site_idCC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 134
ChainResidue
BGLY50
BGOL507

site_idCC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 135
ChainResidue
BARG19
BHOH149
BHOH171
BHOH191
BHOH207
BHOH303
BHOH336

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:A0A0H3AMJ9
ChainResidueDetails
AASP12
BASP12

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:8176739, ECO:0007744|PDB:1CHN
ChainResidueDetails
AASP13
AASP57
AASN59
BASP13
BASP57
BASN59

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:1869568, ECO:0000269|PubMed:2689446
ChainResidueDetails
AASP57
BASP57

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:11359578, ECO:0000269|PubMed:9560203
ChainResidueDetails
ALYS92
BLYS92

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:1390767, ECO:0000269|PubMed:9560203
ChainResidueDetails
ALYS109
BLYS109

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PDB entries from 2024-07-24

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