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Espg structure

Analyse Espg structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FMA
Type: protein
Length: 4,153 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Espg protein
UniProt: Q5WMC0
Ligands: MG
Pockets: 20 · best druggability 0.72

Structure

x-ray diffraction · 11 distinct chains · 34% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Espg protein	protein	351	33% helix, 25% strand	Q5WMC0
C	Espg protein	protein	346	34% helix, 25% strand	Q5WMC0
D	Espg protein	protein	341	34% helix, 25% strand	Q5WMC0
E	Espg protein	protein	349	34% helix, 25% strand	Q5WMC0
F	Espg protein	protein	344	34% helix, 25% strand	Q5WMC0
G	Espg protein	protein	343	33% helix, 25% strand	Q5WMC0
H	Espg protein	protein	347	34% helix, 25% strand	Q5WMC0
I	Espg protein	protein	348	35% helix, 25% strand	Q5WMC0
J	Espg protein	protein	341	35% helix, 25% strand	Q5WMC0
K	Espg protein	protein	344	34% helix, 26% strand	Q5WMC0
L	Espg protein	protein	348	33% helix, 25% strand	Q5WMC0

Ligands and binding sites

MG · Magnesium ion · metal · 19 copies · chains A, B, C, D, K, E, F, H, I, J, L
FMT · Formic acid · additive · 6 copies · chains A, E, B, H, D, L
ACY · Acetic acid · additive · chains J

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	449	0.72	0.82	82	empty
2	855	0.71	0.76	67	empty
3	590	0.70	0.78	69	empty
4	546	0.68	0.78	68	MG
5	483	0.67	0.79	82	empty

Interfaces

17 interfaces between chains.

E–I · 1298 Å² buried · 24 hydrogen bonds · protein-protein
H–J · 1228 Å² buried · 22 hydrogen bonds · protein-protein
I–K · 1108 Å² buried · 16 hydrogen bonds · protein-protein
D–K · 1102 Å² buried · 14 hydrogen bonds · protein-protein
B–H · 1092 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

4FMA · EspG structure · 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 Q5WMC0
Elsewhere: RCSB PDB 4FMA · PDBe 4FMA · UniProt Q5WMC0

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