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6CZM

Crystal structure of Medicago truncatula ATP-phosphoribosyltransferase in tense form

Functional Information from GO Data
ChainGOidnamespacecontents
A0000105biological_processhistidine biosynthetic process
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003879molecular_functionATP phosphoribosyltransferase activity
A0005737cellular_componentcytoplasm
A0008652biological_processamino acid biosynthetic process
A0016757molecular_functionglycosyltransferase activity
B0000105biological_processhistidine biosynthetic process
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003879molecular_functionATP phosphoribosyltransferase activity
B0005737cellular_componentcytoplasm
B0008652biological_processamino acid biosynthetic process
B0016757molecular_functionglycosyltransferase activity
C0000105biological_processhistidine biosynthetic process
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0003879molecular_functionATP phosphoribosyltransferase activity
C0005737cellular_componentcytoplasm
C0008652biological_processamino acid biosynthetic process
C0016757molecular_functionglycosyltransferase activity
D0000105biological_processhistidine biosynthetic process
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0003879molecular_functionATP phosphoribosyltransferase activity
D0005737cellular_componentcytoplasm
D0008652biological_processamino acid biosynthetic process
D0016757molecular_functionglycosyltransferase activity
E0000105biological_processhistidine biosynthetic process
E0000166molecular_functionnucleotide binding
E0000287molecular_functionmagnesium ion binding
E0003879molecular_functionATP phosphoribosyltransferase activity
E0005737cellular_componentcytoplasm
E0008652biological_processamino acid biosynthetic process
E0016757molecular_functionglycosyltransferase activity
F0000105biological_processhistidine biosynthetic process
F0000166molecular_functionnucleotide binding
F0000287molecular_functionmagnesium ion binding
F0003879molecular_functionATP phosphoribosyltransferase activity
F0005737cellular_componentcytoplasm
F0008652biological_processamino acid biosynthetic process
F0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue AMP A 401
ChainResidue
AASP212
ALEU213
ASER215
ASER216
AGLY217
ATHR218
ATHR219

site_idAC2
Number of Residues12
Detailsbinding site for residue HIS A 402
ChainResidue
AGLN302
AGLY303
ATHR305
AVAL325
AILE326
ACYS327
CVAL277
CASN279
CGLY347
CLEU349
AGLY300
ALEU301

site_idAC3
Number of Residues9
Detailsbinding site for residue AMP B 401
ChainResidue
BGLY132
BCYS134
BASP212
BLEU213
BSER215
BSER216
BGLY217
BTHR218
BTHR219

site_idAC4
Number of Residues10
Detailsbinding site for residue HIS B 402
ChainResidue
AVAL277
AASN279
AGLY347
BGLY300
BLEU301
BGLN302
BGLY303
BTHR305
BVAL325
BCYS327

site_idAC5
Number of Residues8
Detailsbinding site for residue AMP C 401
ChainResidue
AASN69
CASP212
CLEU213
CSER215
CSER216
CGLY217
CTHR218
CTHR219

site_idAC6
Number of Residues11
Detailsbinding site for residue HIS C 402
ChainResidue
BVAL277
BASN279
BGLY347
BLEU349
CGLY300
CLEU301
CGLN302
CGLY303
CTHR305
CVAL325
CCYS327

site_idAC7
Number of Residues11
Detailsbinding site for residue AMP D 401
ChainResidue
DCYS134
DASP212
DLEU213
DVAL214
DSER215
DSER216
DGLY217
DTHR218
DTHR219
EVAL68
EASN69

site_idAC8
Number of Residues11
Detailsbinding site for residue HIS D 402
ChainResidue
DGLY300
DLEU301
DGLN302
DGLY303
DTHR305
DVAL325
DCYS327
FVAL277
FASN279
FGLY347
FLEU349

site_idAC9
Number of Residues10
Detailsbinding site for residue AMP E 401
ChainResidue
ECYS134
EGLU199
EASP212
ELEU213
ESER215
ESER216
EGLY217
ETHR218
ETHR219
FASN69

site_idAD1
Number of Residues13
Detailsbinding site for residue HIS E 402
ChainResidue
EVAL325
EILE326
ECYS327
DVAL277
DASN279
DVAL309
DGLY347
DLEU349
EGLY300
ELEU301
EGLN302
EGLY303
ETHR305

site_idAD2
Number of Residues8
Detailsbinding site for residue AMP F 401
ChainResidue
FCYS134
FLEU213
FSER215
FSER216
FGLY217
FTHR218
FTHR219
FHOH501

site_idAD3
Number of Residues11
Detailsbinding site for residue HIS F 402
ChainResidue
EVAL277
EASN279
EGLY347
ELEU349
FGLY300
FLEU301
FGLN302
FGLY303
FTHR305
FVAL325
FCYS327

Functional Information from PROSITE/UniProt
site_idPS01316
Number of Residues22
DetailsATP_P_PHORIBOSYLTR ATP phosphoribosyltransferase signature. EaapamGiAdaIlDLvsSGtTL
ChainResidueDetails
AGLU199-LEU220

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PDB entries from 2024-06-12

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