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Crystal structure of the uncharacterized protein Q2CBJ1_9RHOB from oceanicola granulosus HTCC2516

Analyse Crystal structure of the uncharacterized protein Q2CBJ1_9RHOB from oceanicola… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2RG4
Type: protein
Length: 412 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: Q2CBJ1
Ligands: FE
Pockets: 5 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Uncharacterized protein	protein	206	28% helix, 26% strand	Q2CBJ1

Ligands and binding sites

FE · Fe (III) ion · metal · 2 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, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	728	0.73	0.79	62	FE
2	641	0.73	0.80	68	FE
3	152	0.57	0.82	18	empty
4	203	0.55	0.79	19	empty
5	151	0.48	0.78	21	empty

Interfaces

1 interface between chains.

A–B · 927 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

2RG4 · Crystal structure of the uncharacterized protein Q2CBJ1_9RHOB from Oceanicola granulosus… · 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 Q2CBJ1
Elsewhere: RCSB PDB 2RG4 · PDBe 2RG4 · UniProt Q2CBJ1

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