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Crystal structure of osmc from E. COLI

Analyse Crystal structure of osmc from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1NYE
Type: protein
Length: 910 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Osmotically inducible protein C
UniProt: P0C0L2
Pockets: 9 · best druggability 0.53

Structure

x-ray diffraction · 5 distinct chains · 30% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Osmotically inducible protein C	protein	143	32% helix, 39% strand	P0C0L2
C	Osmotically inducible protein C	protein	153	30% helix, 37% strand	P0C0L2
D	Osmotically inducible protein C	protein	162	29% helix, 34% strand	P0C0L2
E	Osmotically inducible protein C	protein	151	30% helix, 36% strand	P0C0L2
F	Osmotically inducible protein C	protein	158	28% helix, 39% strand	P0C0L2

Pockets

9 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	199	0.53	0.77	25	empty
2	214	0.50	0.76	27	empty
3	182	0.50	0.77	22	empty
4	171	0.50	0.77	23	empty
5	250	0.50	0.74	30	empty

Interfaces

10 interfaces between chains.

C–D · 3360 Å² buried · 62 hydrogen bonds · protein-protein
E–F · 3283 Å² buried · 57 hydrogen bonds · protein-protein
A–B · 3277 Å² buried · 58 hydrogen bonds · protein-protein
B–F · 890 Å² buried · 11 hydrogen bonds · protein-protein
A–D · 834 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

1NYE · Crystal structure of OsmC from E. coli · the same entry in another collection · chain F against F, TM-score 1.00
P0C0L2 · AlphaFold monomer V2.0 prediction for peroxiredoxin osmc (P0C0L2) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P0C0L2
Elsewhere: RCSB PDB 1NYE · PDBe 1NYE · UniProt P0C0L2

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