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Structure of reduced C22S ohrr from xanthamonas campestris

Analyse Structure of reduced C22S ohrr from xanthamonas campestris in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2PEX
Type: protein
Length: 273 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcriptional regulator ohrr
UniProt: Q93R11
Pockets: 3 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 71% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transcriptional regulator ohrr	protein	136	69% helix, 7% strand	Q93R11
B	Transcriptional regulator ohrr	protein	137	74% helix, 5% strand	Q93R11

Ligands and binding sites

FMT · Formic acid · additive · 7 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	90	0.41	0.78	16	FMT
2	99	0.41	0.77	16	FMT
3	94	0.40	0.77	21	empty

Interfaces

1 interface between chains.

A–B · 2839 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

2PEX · Structure of reduced C22S OhrR from Xanthamonas Campestris · 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 Q93R11
Elsewhere: RCSB PDB 2PEX · PDBe 2PEX · UniProt Q93R11

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