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6YMZ

Structure of the CheB methylsterase from P. atrosepticum SCRI1043

Functional Information from GO Data
ChainGOidnamespacecontents
A0000156molecular_functionphosphorelay response regulator activity
A0000160biological_processphosphorelay signal transduction system
A0005737cellular_componentcytoplasm
A0006935biological_processchemotaxis
A0008984molecular_functionprotein-glutamate methylesterase activity
A0016787molecular_functionhydrolase activity
A0050568molecular_functionprotein-glutamine glutaminase activity
B0000156molecular_functionphosphorelay response regulator activity
B0000160biological_processphosphorelay signal transduction system
B0005737cellular_componentcytoplasm
B0006935biological_processchemotaxis
B0008984molecular_functionprotein-glutamate methylesterase activity
B0016787molecular_functionhydrolase activity
B0050568molecular_functionprotein-glutamine glutaminase activity
C0000156molecular_functionphosphorelay response regulator activity
C0000160biological_processphosphorelay signal transduction system
C0005737cellular_componentcytoplasm
C0006935biological_processchemotaxis
C0008984molecular_functionprotein-glutamate methylesterase activity
C0016787molecular_functionhydrolase activity
C0050568molecular_functionprotein-glutamine glutaminase activity
D0000156molecular_functionphosphorelay response regulator activity
D0000160biological_processphosphorelay signal transduction system
D0005737cellular_componentcytoplasm
D0006935biological_processchemotaxis
D0008984molecular_functionprotein-glutamate methylesterase activity
D0016787molecular_functionhydrolase activity
D0050568molecular_functionprotein-glutamine glutaminase activity
E0000156molecular_functionphosphorelay response regulator activity
E0000160biological_processphosphorelay signal transduction system
E0005737cellular_componentcytoplasm
E0006935biological_processchemotaxis
E0008984molecular_functionprotein-glutamate methylesterase activity
E0016787molecular_functionhydrolase activity
E0050568molecular_functionprotein-glutamine glutaminase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ACT A 401
ChainResidue
AGLU98
ATHR169
AGLU170
AARG173
APHE200

site_idAC2
Number of Residues3
Detailsbinding site for residue NA A 402
ChainResidue
AASN205
ACYS208
AILE210

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 403
ChainResidue
AASP326
AGLU327
AVAL328
AHOH530
AVAL325

site_idAC4
Number of Residues4
Detailsbinding site for residue NA A 404
ChainResidue
ALYS3
AASN24
AHIS26
AMET29

site_idAC5
Number of Residues7
Detailsbinding site for residue GOL A 405
ChainResidue
APRO152
AARG349
AILE350
AHOH548
AHOH569
BARG220
CARG220

site_idAC6
Number of Residues5
Detailsbinding site for residue NA B 401
ChainResidue
BLYS3
BASN24
BHIS26
BMET29
BHOH579

site_idAC7
Number of Residues4
Detailsbinding site for residue NA B 402
ChainResidue
BASN205
BCYS208
BILE210
BHOH589

site_idAC8
Number of Residues6
Detailsbinding site for residue GOL C 401
ChainResidue
AARG220
CALA347
CLEU348
CARG349
CHOH547
DARG220

site_idAC9
Number of Residues4
Detailsbinding site for residue NA C 402
ChainResidue
CMET192
CGLY231
CARG258
CPRO259

site_idAD1
Number of Residues4
Detailsbinding site for residue NA C 403
ChainResidue
CASN205
CCYS208
CILE210
CHOH609

site_idAD2
Number of Residues7
Detailsbinding site for residue GOL C 404
ChainResidue
CLYS132
CARG134
CGLU307
CCYS310
CVAL311
CVAL312
CPHE313

site_idAD3
Number of Residues3
Detailsbinding site for residue NA D 401
ChainResidue
DASN205
DCYS208
DILE210

site_idAD4
Number of Residues8
Detailsbinding site for residue GOL D 402
ChainResidue
DASP103
DPHE104
DLYS126
DSER165
DGLN190
DHIS191
DHOH502
DHOH543

site_idAD5
Number of Residues4
Detailsbinding site for residue NA E 401
ChainResidue
EASN205
ECYS208
EGLN209
EILE210

site_idAD6
Number of Residues5
Detailsbinding site for residue SO4 E 402
ChainResidue
CVAL325
CASP326
CVAL328
EGLU202
ELYS206

site_idAD7
Number of Residues4
Detailsbinding site for residue GOL E 403
ChainResidue
EASP11
EARG247
ETYR271
EHOH537

site_idAD8
Number of Residues6
Detailsbinding site for residue GOL E 404
ChainResidue
EVAL31
ETHR34
EARG266
EALA290
ELEU293
EGLU294

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues15
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00099
ChainResidueDetails
BSER165
BHIS191
BASP287
CSER165
CHIS191
CASP287
DSER165
DHIS191
DASP287
ESER165
EHIS191
EASP287
ASER165
AHIS191
AASP287

site_idSWS_FT_FI2
Number of Residues5
DetailsMOD_RES: 4-aspartylphosphate => ECO:0000255|HAMAP-Rule:MF_00099
ChainResidueDetails
BASP56
CASP56
DASP56
EASP56
AASP56

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PDB entries from 2024-06-12

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