Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3FGZ

Crystal Structure of CheY triple mutant F14E, N59M, E89R complexed with BeF3- and Mn2+

Replaces:  2J8E
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 MN A 202
ChainResidue
AASP13
AASP57
AMET59
ABEF130
AHOH151
AHOH192

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BEF A 130
ChainResidue
ATHR87
AALA88
ALYS109
AHOH151
AHOH156
AMN202
AASP57
ATRP58
AMET59

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 501
ChainResidue
AARG19
ALYS70
BLYS126

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 202
ChainResidue
BASP13
BASP57
BMET59
BBEF130
BHOH147
BHOH178

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BEF B 130
ChainResidue
BASP57
BTRP58
BMET59
BTHR87
BALA88
BLYS109
BHOH178
BMN202

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 500
ChainResidue
BARG19
BHOH148
BHOH185

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NH4 B 502
ChainResidue
BMET17
BGLN47

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
AMET59
BASP13
BASP57
BMET59

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

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon