MolNFT v1 · #80647 · protein

Crystal structure of the general stress FMN/FAD binding protein from the phytopathogen xanthomonas citri

3U34 · General stress protein: “Crystal structure of the general stress FMN/FAD binding protein from the phytopathogen xanthomonas citri”. X-ray diffraction, 6 pockets (best druggability 0.83). MolNFT v1 #80647 on GenesisL1: 3D structure…

PDB: 3U34
Type: protein
Length: 566 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: General stress protein
UniProt: Q8PK08
Pockets: 6 · best druggability 0.83

Structure

x-ray diffraction · 3 distinct chains · 25% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	General stress protein	protein	142	25% helix, 43% strand	Q8PK08
B, D	General stress protein	protein	141	25% helix, 43% strand	Q8PK08
C	General stress protein	protein	142	25% helix, 43% strand	Q8PK08

Ligands and binding sites

PGE · Triethylene glycol · additive · 2 copies · chains A, B, C, D

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

Pockets

6 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	670	0.83	0.87	96	empty
2	50	0.64	0.95	17	empty
3	126	0.62	0.86	26	empty
4	195	0.61	0.83	30	empty
5	196	0.60	0.82	29	empty

Interfaces

6 interfaces between chains.

A–D · 1336 Å² buried · 29 hydrogen bonds · protein-protein
B–C · 1267 Å² buried · 22 hydrogen bonds · protein-protein
C–D · 1064 Å² buried · 13 hydrogen bonds · protein-protein
A–B · 1063 Å² buried · 13 hydrogen bonds · protein-protein
B–D · 621 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

3U34 · Crystal structure of the general stress FMN/FAD binding protein from the phytopathogen… · 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 Q8PK08
Elsewhere: RCSB PDB 3U34 · PDBe 3U34 · UniProt Q8PK08

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