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Crystal structure of metal-free human arginase I

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

PDB: 3TF3
Type: protein
Length: 628 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
Pockets: 3 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Arginase-1 (EC 3.5.3.1)	protein	314	43% helix, 17% strand	P05089

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1038	0.77	0.80	89	empty
2	94	0.44	0.80	20	empty
3	54	0.37	0.80	16	empty

Interfaces

1 interface between chains.

A–B · 433 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

3TF3 · Crystal structure of metal-free Human Arginase I · the same entry in another collection · chain A against A, 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 3TF3 · PDBe 3TF3 · UniProt P05089

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