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Crystal structure of human arginase I from twinned crystal

Analyse Crystal structure of human arginase I from twinned crystal in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WVA
Type: protein
Length: 618 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Arginase 1
EC: 3.5.3.1
UniProt: P05089
Ligands: S2C, MN
Pockets: 3 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Arginase 1 (EC 3.5.3.1)	protein	309	43% helix, 16% strand	P05089

Ligands and binding sites

S2C · S-2-(boronoethyl)-L-cysteine · ligand · 2 copies · chains A, B
MN · Manganese (II) ion · metal · 4 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	78	0.44	0.81	20	S2C
2	85	0.43	0.80	19	S2C
3	57	0.35	0.78	15	empty

Compared structures

1WVA · Crystal structure of human arginase I from twinned crystal · the same entry in another collection · chain B against B, TM-score 1.00
P05089 · AlphaFold monomer V2.0 prediction for arginase-1 (P05089) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P05089
Elsewhere: RCSB PDB 1WVA · PDBe 1WVA · UniProt P05089

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