Structure of PDB 1uu1 Chain A

Receptor sequence
>1uu1A (length=329) Species: 2336 (Thermotoga maritima) [Search protein sequence]
LIAKRAYPYETEKRDKTYLALNENPFPFPEDLVDEVFRRLNSDALRIYYD
SPDEELIEKILSYLDTDFLSKNNVSVGNGADEIIYVMMLMFDRSVFFPPT
YSCYRIFAKAVGAKFLEVPLTKDLRIPEVNVGEGDVVFIPNPNNPTGHVF
EREEIERILKTGAFVALDEAYYEFHGESYVDFLKKYENLAVIRTFSKAFS
LAAQRVGYVVASEKFIDAYNRVRLPFNVSYVSQMFAKVALDHREIFEERT
KFIVEERERMKSALREMGYRITDSRGNFVFVFMEKEEKERLLEHLRTKNV
AVRSFREGVRITIGKREENDMILRELEVF
3D structure
PDB1uu1 Structural Studies of the Catalytic Reaction Pathway of a Hyperthermophilic Histidinol-Phosphate Aminotransferase
ChainA
Resolution2.38 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 PMP A G84 A85 D86 Y106 N149 D173 A175 Y176 T199 S201 K202 R210 G79 A80 D81 Y101 N144 D168 A170 Y171 T194 S196 K197 R205
BS02 HSA A D86 Y106 S107 N149 R315 D81 Y101 S102 N144 R310
BS03 HSA A Y53 F231 Y48 F226
Gene Ontology
Molecular Function
GO:0004400 histidinol-phosphate transaminase activity
GO:0008483 transaminase activity
GO:0016740 transferase activity
GO:0030170 pyridoxal phosphate binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0000105 L-histidine biosynthetic process
GO:0009058 biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1uu1, PDBe:1uu1, PDBj:1uu1
PDBsum1uu1
PubMed15007066
UniProtQ9X0D0|HIS8_THEMA Histidinol-phosphate aminotransferase (Gene Name=hisC)

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