Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3OLV

Structural and functional effects of substitution at position T+1 in CheY: CheYA88V-BeF3-Mg complex

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 Residues6
DetailsBINDING SITE FOR RESIDUE MG A 130
ChainResidue
AASP13
AASP57
AASN59
ABEF131
AHOH136
AHOH137

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BEF A 131
ChainResidue
ATHR87
AVAL88
ALYS109
AMG130
AHOH137
BGLN47
AASP57
ATRP58
AASN59

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 132
ChainResidue
ALYS91
ALYS92
AHOH180
BLYS92

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BEF A 133
ChainResidue
AGLN100
AHOH208
BARG73
BALA80
BSER104

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BEF A 134
ChainResidue
AGLU37
AASP41
ALYS45
AHOH255

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BEF A 135
ChainResidue
AASP13
ASER15
AARG18
AHOH182

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 130
ChainResidue
BASP13
BASP57
BASN59
BBEF131
BHOH135
BHOH159

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BEF B 131
ChainResidue
AGLN47
BASP57
BTRP58
BASN59
BTHR87
BVAL88
BLYS109
BMG130
BHOH135

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 132
ChainResidue
BALA90
BLYS91
BLYS92
BHOH247

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BEF B 133
ChainResidue
BGLU37
BASP41
BLYS45

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

221716

PDB entries from 2024-06-26

PDB statisticsPDBj update infoContact PDBjnumon