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1GEX

CRYSTAL STRUCTURE OF HISTIDINOL-PHOSPHATE AMINOTRANSFERASE COMPLEXED WITH HISTIDINOL-PHOSPHATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000105biological_processhistidine biosynthetic process
A0004400molecular_functionhistidinol-phosphate transaminase activity
A0005829cellular_componentcytosol
A0008483molecular_functiontransaminase activity
A0008652biological_processamino acid biosynthetic process
A0009058biological_processbiosynthetic process
A0016740molecular_functiontransferase activity
A0030170molecular_functionpyridoxal phosphate binding
A0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP A 413
ChainResidue
ATYR55
ATYR187
ATHR211
ASER213
ALYS214
AARG222
AHSA414
AGLY83
AALA84
AASP85
ATYR110
ACYS153
AASN157
AASP184
AALA186

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HSA A 414
ChainResidue
ATYR20
AALA36
ATYR55
AASP85
ATYR110
AASN157
ALYS214
AARG322
AARG335
APLP413
AHOH518

Functional Information from PROSITE/UniProt
site_idPS00599
Number of Residues10
DetailsAA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TLSKAFALAG
ChainResidueDetails
ATHR211-GLY220

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALYS214

218853

PDB entries from 2024-04-24

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