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4YB5

Adenosine triphosphate phosphoribosyltransferase from Campylobacter jejuni in complex with the allosteric inhibitor histidine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000105biological_processL-histidine biosynthetic process
A0000287molecular_functionmagnesium ion binding
A0003879molecular_functionATP phosphoribosyltransferase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0016757molecular_functionglycosyltransferase activity
A0046872molecular_functionmetal ion binding
B0000105biological_processL-histidine biosynthetic process
B0000287molecular_functionmagnesium ion binding
B0003879molecular_functionATP phosphoribosyltransferase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0016757molecular_functionglycosyltransferase activity
B0046872molecular_functionmetal ion binding
C0000105biological_processL-histidine biosynthetic process
C0000287molecular_functionmagnesium ion binding
C0003879molecular_functionATP phosphoribosyltransferase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0016757molecular_functionglycosyltransferase activity
C0046872molecular_functionmetal ion binding
D0000105biological_processL-histidine biosynthetic process
D0000287molecular_functionmagnesium ion binding
D0003879molecular_functionATP phosphoribosyltransferase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0016757molecular_functionglycosyltransferase activity
D0046872molecular_functionmetal ion binding
E0000105biological_processL-histidine biosynthetic process
E0000287molecular_functionmagnesium ion binding
E0003879molecular_functionATP phosphoribosyltransferase activity
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0016757molecular_functionglycosyltransferase activity
E0046872molecular_functionmetal ion binding
F0000105biological_processL-histidine biosynthetic process
F0000287molecular_functionmagnesium ion binding
F0003879molecular_functionATP phosphoribosyltransferase activity
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0016757molecular_functionglycosyltransferase activity
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue SCN A 301
ChainResidue
AASP100
AMET221
AARG224

site_idAC2
Number of Residues2
Detailsbinding site for residue SCN A 302
ChainResidue
AASN181
FPRO159

site_idAC3
Number of Residues3
Detailsbinding site for residue K A 303
ChainResidue
AGLN178
AASN181
FARG160

site_idAC4
Number of Residues11
Detailsbinding site for residue HIS A 304
ChainResidue
AVAL248
AGLU249
AARG250
ATHR252
AHIS266
AMET267
AVAL268
AHOH407
EHIS232
ESER288
AGLY247

site_idAC5
Number of Residues3
Detailsbinding site for residue K A 305
ChainResidue
AARG160
FGLN178
FASN181

site_idAC6
Number of Residues3
Detailsbinding site for residue SCN B 301
ChainResidue
BASP100
BMET221
BARG224

site_idAC7
Number of Residues3
Detailsbinding site for residue K B 302
ChainResidue
BGLN178
BASN181
DARG160

site_idAC8
Number of Residues11
Detailsbinding site for residue HIS B 303
ChainResidue
BGLY247
BVAL248
BGLU249
BARG250
BTHR252
BHIS266
BMET267
BVAL268
CHIS232
CSER288
CHOH403

site_idAC9
Number of Residues2
Detailsbinding site for residue SCN C 301
ChainResidue
CMET221
CARG224

site_idAD1
Number of Residues9
Detailsbinding site for residue PGE C 302
ChainResidue
CSER226
CLEU245
CPRO246
CGLY247
CVAL248
CVAL268
CSER269
CLYS270
CLEU273

site_idAD2
Number of Residues3
Detailsbinding site for residue K C 303
ChainResidue
CGLN178
CASN181
EARG160

site_idAD3
Number of Residues10
Detailsbinding site for residue HIS C 304
ChainResidue
CGLY247
CVAL248
CGLU249
CARG250
CTHR252
CHIS266
CVAL268
FHIS232
FSER288
FHOH404

site_idAD4
Number of Residues3
Detailsbinding site for residue K C 305
ChainResidue
CARG160
EGLN178
EASN181

site_idAD5
Number of Residues6
Detailsbinding site for residue PEG D 301
ChainResidue
DLYS235
DPRO255
DLEU256
DASP259
DASN262
DVAL263

site_idAD6
Number of Residues10
Detailsbinding site for residue HIS D 302
ChainResidue
AHIS232
ASER288
DGLY247
DVAL248
DGLU249
DARG250
DTHR252
DHIS266
DVAL268
DHOH404

site_idAD7
Number of Residues4
Detailsbinding site for residue SCN E 301
ChainResidue
EASP100
EPHE101
EMET221
EARG224

site_idAD8
Number of Residues4
Detailsbinding site for residue SCN E 302
ChainResidue
CPRO111
CPRO159
CHOH413
EASN181

site_idAD9
Number of Residues10
Detailsbinding site for residue HIS E 303
ChainResidue
EHOH405
DHIS232
DSER288
EGLY247
EVAL248
EGLU249
EARG250
ETHR252
EHIS266
EVAL268

site_idAE1
Number of Residues3
Detailsbinding site for residue SCN F 301
ChainResidue
FASP100
FMET221
FARG224

site_idAE2
Number of Residues3
Detailsbinding site for residue SCN F 302
ChainResidue
DHIS258
FLYS186
FVAL187

site_idAE3
Number of Residues9
Detailsbinding site for residue PEG F 303
ChainResidue
FVAL220
FALA223
FARG224
FGLU225
FSER226
FLYS227
FPRO293
FILE294
FGLU295

site_idAE4
Number of Residues12
Detailsbinding site for residue HIS F 304
ChainResidue
BHIS232
BSER288
BLEU290
FGLY247
FVAL248
FGLU249
FARG250
FTHR252
FHIS266
FMET267
FVAL268
FHOH403

Functional Information from PROSITE/UniProt
site_idPS01316
Number of Residues22
DetailsATP_P_PHORIBOSYLTR ATP phosphoribosyltransferase signature. EvapraNlAdaIcDLvsSGaTL
ChainResidueDetails
AGLU156-LEU177

226707

PDB entries from 2024-10-30

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