Structure of PDB 1fg3 Chain A

Receptor sequence
>1fg3A (length=354) Species: 562 (Escherichia coli) [Search protein sequence]
TVTITDLARENVRNLTPYQSARRLGGNGDVWLNANEYPTAVEFQLTQQTL
NRYPECQPKAVIENYAQYAGVKPEQVLVSRGADEGIELLIRAFCEPGKDA
ILYCPPTYGMYSVSAETIGVECRTVPTLDNWQLDLQGISDKLDGVKVVYV
CSPNNPTGQLINPQDFRTLLELTRGKAIVVADEAYIEFCPQASLAGWLAE
YPHLAILRTLSKAFALAGLRCGFTLANEEVINLLMKVIAPYPLSTPVADI
AAQALSPQGIVAMRERVAQIIAEREYLIAALKEIPCVEQVFDSETNYILA
RFKASSAVFKSLWDQGIILRDQNKQPSLSGCLRITVGTREESQRVIDALR
AEQV
3D structure
PDB1fg3 Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and l-histidinol phosphate.
ChainA
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.6.1.9: histidinol-phosphate transaminase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 PLP A G83 A84 D85 Y110 N157 D184 A186 Y187 T211 S213 K214 R222 G81 A82 D83 Y108 N155 D182 A184 Y185 T209 S211 K212 R220
BS02 HSA A Y20 A36 D85 Y110 N157 K214 R322 R335 Y18 A34 D83 Y108 N155 K212 R320 R333
Gene Ontology
Molecular Function
GO:0004400 histidinol-phosphate transaminase activity
GO:0008483 transaminase activity
GO:0016740 transferase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
Biological Process
GO:0000105 L-histidine biosynthetic process
GO:0009058 biosynthetic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:1fg3, PDBe:1fg3, PDBj:1fg3
PDBsum1fg3
PubMed11518529
UniProtP06986|HIS8_ECOLI Histidinol-phosphate aminotransferase (Gene Name=hisC)

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