Structure of PDB 3k5h Chain D

Receptor sequence
>3k5hD (length=380) Species: 5057 (Aspergillus clavatus) [Search protein sequence]
WNSRKVGVLGGGQLGRMLVESANRLNIQVNVLDADNSPAKQISAHDGHVT
GSFKEREAVRQLAKTCDVVTAEIEHVDTYALEEVASEVKIEPSWQAIRTI
QNKFNQKEHLRKYGIPMAEHRELVENTPAELAKVGEQLGYPLMLKSKTMA
YDGRGNFRVNSQDDIPEALEALKDRPLYAEKWAYFKMELAVIVVKTKDEV
LSYPTVETVQEDSICKLVYAPARNVSDAINQKAQELARKAVAAFDGKGVF
GVEMFLLEDDSIMLCEIASRIHNSGHYTIEGCALSQFDAHLRAILDLPIP
AQSLEIRQPSIMLNIIGGAAPDTHLQAAECALSIPNASIHLYSKGAAKPG
RKMGHITVTAPTMHEAETHIQPLIDVVDRI
3D structure
PDB3k5h Structural and functional studies of Aspergillus clavatus N(5)-carboxyaminoimidazole ribonucleotide synthetase
ChainD
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y152 G154 E254 E267 N274 S275 K353
Catalytic site (residue number reindexed from 1) Y151 G153 E253 E266 N273 S274 K352
Enzyme Commision number 4.1.1.21: phosphoribosylaminoimidazole carboxylase.
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 ATP D K104 M144 K146 Y152 D153 G154 E181 W183 A184 E189 E254 F256 E267 K103 M143 K145 Y151 D152 G153 E180 W182 A183 E188 E253 F255 E266
BS02 MG D E254 E267 E253 E266
Gene Ontology
Molecular Function
GO:0004638 phosphoribosylaminoimidazole carboxylase activity
GO:0005524 ATP binding
GO:0046872 metal ion binding
Biological Process
GO:0006189 'de novo' IMP biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3k5h, PDBe:3k5h, PDBj:3k5h
PDBsum3k5h
PubMed20050602
UniProtA1CII2

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