MolNFT v1 · #129820 · protein

Cupriavidus metallidurans bph

5OVU · Beta-proteobacteria proteasome homologue: “Cupriavidus metallidurans bph”. X-ray diffraction, 5 pockets (best druggability 0.54). MolNFT v1 #129820 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5OVU
Type: protein
Length: 371 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-proteobacteria proteasome homologue
UniProt: Q1LP42
Pockets: 5 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-proteobacteria proteasome homologue	protein	186	34% helix, 28% strand	Q1LP42
B	Beta-proteobacteria proteasome homologue	protein	185	34% helix, 29% strand	Q1LP42

Ligands and binding sites

MLI · Malonate ion · additive · 4 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	230	0.54	0.77	33	empty
2	146	0.50	0.79	21	empty
3	63	0.40	0.79	14	MLI
4	63	0.38	0.78	14	MLI
5	71	0.32	0.75	21	empty

Interfaces

1 interface between chains.

A–B · 631 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

5OVU · Cupriavidus metallidurans BPH · 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 Q1LP42
Elsewhere: RCSB PDB 5OVU · PDBe 5OVU · UniProt Q1LP42

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