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Crystal structure of an uncharacterized protein A6V7T0 from pseudomonas aeruginosa

Analyse Crystal structure of an uncharacterized protein A6V7T0 from pseudomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3K12
Type: protein
Length: 693 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein A6V7T0
UniProt: Q9I3E9
Pockets: 11 · best druggability 0.86

Structure

x-ray diffraction · 3 distinct chains · 28% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, E	Uncharacterized protein A6V7T0	protein	115	28% helix, 40% strand	Q9I3E9
B, F	Uncharacterized protein A6V7T0	protein	114	28% helix, 39% strand	Q9I3E9
D	Uncharacterized protein A6V7T0	protein	120	27% helix, 34% strand	Q9I3E9

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains C, D, B, E

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

Pockets

11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	293	0.86	0.97	39	empty
2	285	0.86	0.97	39	empty
3	1112	0.78	0.80	79	GOL
4	77	0.39	0.79	22	empty
5	80	0.38	0.77	17	empty

Interfaces

9 interfaces between chains.

A–B · 1253 Å² buried · 31 hydrogen bonds · protein-protein
A–C · 1123 Å² buried · 18 hydrogen bonds · protein-protein
C–D · 1122 Å² buried · 19 hydrogen bonds · protein-protein
E–F · 1089 Å² buried · 18 hydrogen bonds · protein-protein
B–F · 1086 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

3K12 · Crystal structure of an uncharacterized protein A6V7T0 from Pseudomonas aeruginosa · 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 Q9I3E9
Elsewhere: RCSB PDB 3K12 · PDBe 3K12 · UniProt Q9I3E9

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