Structure of PDB 3ax6 Chain D

Receptor sequence
>3ax6D (length=359) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence]
MKKIGIIGGGQLGKMMTLEAKKMGFYVIVLDPTPRSPAGQVADEQIVAGF
FDSERIEDLVKGSDVTTYDLEHIDVQTLKKLYNEGYKIHPSPYTLEIIQD
KFVQKEFLKKNGIPVPEYKLVKDLESDVREFGFPVVQKARKGVFIIKNEK
DLENAIKGETYLEEFVEIEKELAVMVARNEKGEIACYPVVEMYDTVIAPA
RIEEKYSKIAREIATSVVEALEGVGIFGIEMFLTKQGEILVNEIAPRPHN
SGHYTIEACVTSQFEQHIRAIMNLPLGSTELLIPAVMVNLLGEEGYYGKP
ALIGLEEALAIEGLSLHFYGKKETRPYRKMGHFTVVDRDVERALEKALRA
KKILKVVSE
3D structure
PDB3ax6 Crystal structures of N5-carboxyaminoimidazole ribonucleotide synthetase, PurK, from thermophilic bacteria
ChainD
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E244 E257 N264 S265 K343
Catalytic site (residue number reindexed from 1) E230 E243 N250 S251 K329
Enzyme Commision number 6.3.4.18: 5-(carboxyamino)imidazole ribonucleotide synthase.
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 ADP D K138 E169 F171 V172 E177 K138 E163 F165 V166 E171
Gene Ontology
Molecular Function
GO:0004638 phosphoribosylaminoimidazole carboxylase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0034028 5-(carboxyamino)imidazole ribonucleotide synthase activity
GO:0046872 metal ion binding
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3ax6, PDBe:3ax6, PDBj:3ax6
PDBsum3ax6
PubMed
UniProtQ9WYS8

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