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3GET

Crystal structure of putative histidinol-phosphate aminotransferase (NP_281508.1) from Campylobacter jejuni at 2.01 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000105biological_processL-histidine biosynthetic process
A0004400molecular_functionhistidinol-phosphate transaminase activity
A0008483molecular_functiontransaminase activity
A0008652biological_processamino acid biosynthetic process
A0009058biological_processbiosynthetic process
A0016740molecular_functiontransferase activity
A0030170molecular_functionpyridoxal phosphate binding
B0000105biological_processL-histidine biosynthetic process
B0004400molecular_functionhistidinol-phosphate transaminase activity
B0008483molecular_functiontransaminase activity
B0008652biological_processamino acid biosynthetic process
B0009058biological_processbiosynthetic process
B0016740molecular_functiontransferase activity
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IPA A 365
ChainResidue
ALYS101
AASN103
AASP184

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IPA B 365
ChainResidue
BLYS101
BASN103
BASP184
BHOH765

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL B 366
ChainResidue
AASN256
AVAL257
ASER258
BLEU233
BARG234
BASN256
BVAL257
BSER258
BHOH511
ALEU233
AARG234

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01023","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
APHE115
AASP190

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BPHE115
BASP190

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PDB entries from 2025-12-24

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