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1H3D

STRUCTURE OF THE E.COLI ATP-PHOSPHORIBOSYLTRANSFERASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000105biological_processL-histidine biosynthetic process
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003879molecular_functionATP phosphoribosyltransferase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE AMP A 400
ChainResidue
AARG16
ATHR176
ACYS104
AGLU156
AASP169
ALEU170
ASER172
ATHR173
AGLY174
AALA175

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE TLA A 410
ChainResidue
AALA26
AARG27
AGLY29
APHE274
ATRP275
ALYS296

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE TLA A 411
ChainResidue
ATYR93
ATHR95

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

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PDB entries from 2025-06-11

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