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4GUD

Crystal Structure of Amidotransferase HisH from Vibrio cholerae

Functional Information from GO Data
ChainGOidnamespacecontents
A0000105biological_processhistidine biosynthetic process
A0000107molecular_functionimidazoleglycerol-phosphate synthase activity
A0004359molecular_functionglutaminase activity
A0005737cellular_componentcytoplasm
A0006541biological_processglutamine metabolic process
A0008652biological_processamino acid biosynthetic process
A0016763molecular_functionpentosyltransferase activity
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
B0000105biological_processhistidine biosynthetic process
B0000107molecular_functionimidazoleglycerol-phosphate synthase activity
B0004359molecular_functionglutaminase activity
B0005737cellular_componentcytoplasm
B0006541biological_processglutamine metabolic process
B0008652biological_processamino acid biosynthetic process
B0016763molecular_functionpentosyltransferase activity
B0016787molecular_functionhydrolase activity
B0016829molecular_functionlyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
ATRP125
AARG188
AHOH426

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG A 302
ChainResidue
ATRP125
BSER151

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 1PE B 301
ChainResidue
BEDO302
ASER151
BTRP125
BTYR147
BARG188

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO B 302
ChainResidue
B1PE301

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
ACYS79
BCYS79

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AHIS185
AGLU187
BHIS185
BGLU187

219869

PDB entries from 2024-05-15

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