Structure of PDB 3k5h Chain A

Receptor sequence
>3k5hA (length=382) Species: 5057 (Aspergillus clavatus) [Search protein sequence]
MWNSRKVGVLGGGQLGRMLVESANRLNIQVNVLDADNSPAKQISAHDGHV
TGSFKEREAVRQLAKTCDVVTAEIEHVDTYALEEVASEVKIEPSWQAIRT
IQNKFNQKEHLRKYGIPMAEHRELVENTPAELAKVGEQLGYPLMLKSKTM
AYDGRGNFRVNSQDDIPEALEALKDRPLYAEKWAYFKMELAVIVVKTKDE
VLSYPTVETVQEDSICKLVYAPARNVSDAINQKAQELARKAVAAFDGKGV
FGVEMFLLEDDSIMLCEIASRIHNSGHYTIEGCALSQFDAHLRAILDLPI
PAQSLEIRQPSIMLNIIGGAAPDTHLQAAECALSIPNASIHLYSKGAAKP
GRKMGHITVTAPTMHEAETHIQPLIDVVDRIR
3D structure
PDB3k5h Structural and functional studies of Aspergillus clavatus N(5)-carboxyaminoimidazole ribonucleotide synthetase
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) Y152 G154 E254 E267 N274 S275 K353
Catalytic site (residue number reindexed from 1) Y152 G154 E254 E267 N274 S275 K353
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 A K104 K146 Y152 D153 G154 N157 E181 W183 A184 F186 E189 E254 F256 E267 K104 K146 Y152 D153 G154 N157 E181 W183 A184 F186 E189 E254 F256 E267
BS02 MG A E254 E267 E254 E267
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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3k5h, PDBe:3k5h, PDBj:3k5h
PDBsum3k5h
PubMed20050602
UniProtA1CII2

[Back to BioLiP]