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6CZL

Crystal structure of Medicago truncatula ATP-phosphoribosyltransferase in relaxed form

Functional Information from GO Data
ChainGOidnamespacecontents
A0000105biological_processL-histidine biosynthetic process
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003879molecular_functionATP phosphoribosyltransferase activity
A0005737cellular_componentcytoplasm
A0016757molecular_functionglycosyltransferase activity
B0000105biological_processL-histidine biosynthetic process
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003879molecular_functionATP phosphoribosyltransferase activity
B0005737cellular_componentcytoplasm
B0016757molecular_functionglycosyltransferase activity
C0000105biological_processL-histidine biosynthetic process
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0003879molecular_functionATP phosphoribosyltransferase activity
C0005737cellular_componentcytoplasm
C0016757molecular_functionglycosyltransferase activity
D0000105biological_processL-histidine biosynthetic process
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0003879molecular_functionATP phosphoribosyltransferase activity
D0005737cellular_componentcytoplasm
D0016757molecular_functionglycosyltransferase activity
E0000105biological_processL-histidine biosynthetic process
E0000166molecular_functionnucleotide binding
E0000287molecular_functionmagnesium ion binding
E0003879molecular_functionATP phosphoribosyltransferase activity
E0005737cellular_componentcytoplasm
E0016757molecular_functionglycosyltransferase activity
F0000105biological_processL-histidine biosynthetic process
F0000166molecular_functionnucleotide binding
F0000287molecular_functionmagnesium ion binding
F0003879molecular_functionATP phosphoribosyltransferase activity
F0005737cellular_componentcytoplasm
F0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue CL A 401
ChainResidue
ATHR219

site_idAC2
Number of Residues4
Detailsbinding site for residue CL B 401
ChainResidue
BSER215
BSER216
BGLY217
BTHR219

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL B 402
ChainResidue
BGLN72
BSER46
BSER51
BGLN67
BPRO70

site_idAC4
Number of Residues4
Detailsbinding site for residue CL C 401
ChainResidue
CSER215
CGLY217
CTHR219
CHOH501

site_idAC5
Number of Residues4
Detailsbinding site for residue GOL C 402
ChainResidue
CSER46
CGLN67
CPRO70
CGLN72

site_idAC6
Number of Residues4
Detailsbinding site for residue CL D 401
ChainResidue
DSER215
DSER216
DGLY217
DTHR219

site_idAC7
Number of Residues2
Detailsbinding site for residue GOL D 402
ChainResidue
DSER46
DGLN72

site_idAC8
Number of Residues3
Detailsbinding site for residue CL E 401
ChainResidue
ESER216
EGLY217
ETHR219

site_idAC9
Number of Residues5
Detailsbinding site for residue GOL E 402
ChainResidue
ESER46
ESER51
EGLN67
EPRO70
EGLN72

site_idAD1
Number of Residues4
Detailsbinding site for residue CL F 401
ChainResidue
FVAL214
FGLY217
FTHR218
FTHR219

site_idAD2
Number of Residues5
Detailsbinding site for residue GOL F 402
ChainResidue
FSER46
FGLN67
FPRO70
FARG71
FGLN72

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

226707

PDB entries from 2024-10-30

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