Structure of PDB 6nfp Chain F

Receptor sequence
>6nfpF (length=289) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
DKTISVIGMPMDLGQARRGVDMGPSAIRYAHLIERLSDMGYTVEDLGDIP
INREELKNLNSVLAGNEKLAQKVNKVIEEKKFPLVLGGDHSIAIGTLAGT
AKHYDNLGVIWYDAHGDLNTLETSPSGNIHGMPLAVSLGIGHESLVNLEG
YAPKIKPENVVIIGARSLDEGERKYIKESGMKVYTMHEIDRLGMTKVIEE
TLDYLSACDGVHLSLDLDGLDPNDAPGVGTPVVGGISYRESHLAMEMLYD
AGIITSAEFVEVNPILDHKNKTGKTAVELVESLLGKKLL
3D structure
PDB6nfp 1.7 Angstrom Resolution Crystal Structure of Arginase from Bacillus subtilis subsp. subtilis str. 168
ChainF
Resolution1.7 Å
3D
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
Enzyme Commision number 3.5.3.1: arginase.
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 MG F D120 H122 D223 D225 D113 H115 D216 D218
BS02 MG F H97 D120 D124 D223 H90 D113 D117 D216
BS03 GOA F Y256 L290 L291 Y249 L283 L284
Gene Ontology
Molecular Function
GO:0004053 arginase activity
GO:0016787 hydrolase activity
GO:0016813 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
Biological Process
GO:0000050 urea cycle
GO:0006525 arginine metabolic process
GO:0019547 arginine catabolic process to ornithine
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6nfp, PDBe:6nfp, PDBj:6nfp
PDBsum6nfp
PubMed
UniProtP39138|ARGI_BACSU Arginase (Gene Name=rocF)

[Back to BioLiP]