Structure of PDB 2we4 Chain D

Receptor sequence
>2we4D (length=309) Species: 1351 (Enterococcus faecalis) [Search protein sequence]
GKKMVVALGGNAILSNDASAHAQQQALVQTSAYLVHLIKQGHRLIVSHGN
GPQVGNLLLQQQAADSEKNPAMPLDTCVAMTQGSIGYWLSNALNQELNKA
GIKKQVATVLTQVVVDPADEAFKNPTKPIGPFLTEAEAKEAMQAGAIFKE
DAGRGWRKVVPSPKPIDIHEAETINTLIKNDIITISCGGGGIPVVGQELK
GVEAVIDKDFASEKLAELVDADALVILTGVDYVCINYGKPDEKQLTNVTV
AELEEYKQAGHFAPGSMLPKIEAAIQFVESQPNKQAIITSLENLGSMSGD
EIVGTVVTK
3D structure
PDB2we4 Substrate Binding and Catalysis in Carbamate Kinase Ascertained by Crystallographic and Site-Directed Mutagenesis Studies. Movements and Significance of a Unique Globular Subdomain of This Key Enzyme for Fermentative ATP Production in Bacteria.
ChainD
Resolution2.02 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G11 N12 K128 K209 K271
Catalytic site (residue number reindexed from 1) G10 N11 K127 K208 K270
Enzyme Commision number 2.7.2.2: carbamate kinase.
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 SO4 D G10 G11 N12 G50 G52 K128 K209 G9 G10 N11 G49 G51 K127 K208
BS02 SO4 D R155 R158 R154 R157
BS03 SO4 D I236 N237 H262 F263 I235 N236 H261 F262
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0008804 carbamate kinase activity
GO:0016301 kinase activity
Biological Process
GO:0006525 arginine metabolic process
GO:0016310 phosphorylation
GO:0019546 arginine deiminase pathway
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2we4, PDBe:2we4, PDBj:2we4
PDBsum2we4
PubMed20188742
UniProtP0A2X7|ARCC1_ENTFA Carbamate kinase 1 (Gene Name=arcC1)

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