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Crystal structure of the arginase from thermus thermophilus

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

PDB: 2EIV
Type: protein
Length: 3,276 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Arginase
UniProt: Q5SI78
Pockets: 20 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, D, E, F, G, H, I, J, K, L, M	Arginase	protein	273	45% helix, 20% strand	Q5SI78

Pockets

20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	453	0.74	0.84	50	empty
2	433	0.63	0.77	44	empty
3	423	0.63	0.77	53	empty
4	337	0.62	0.78	38	empty
5	386	0.61	0.77	50	empty

Interfaces

14 interfaces between chains.

F–H · 684 Å² buried · 10 hydrogen bonds · protein-protein
C–K · 672 Å² buried · 12 hydrogen bonds · protein-protein
A–D · 670 Å² buried · 16 hydrogen bonds · protein-protein
A–H · 670 Å² buried · 13 hydrogen bonds · protein-protein
E–F · 669 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

2EIV · Crystal Structure of the arginase from Thermus thermophilus · the same entry in another collection · 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 Q5SI78
Elsewhere: RCSB PDB 2EIV · PDBe 2EIV · UniProt Q5SI78

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