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Crystal structure of escherichia COLI opgg

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

PDB: 1TXK
Type: protein
Length: 977 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucans biosynthesis protein G
UniProt: P33136
Ligands: NA
Pockets: 13 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glucans biosynthesis protein G	protein	490	7% helix, 45% strand	P33136
B	Glucans biosynthesis protein G	protein	487	7% helix, 46% strand	P33136

Ligands and binding sites

NA · Sodium ion · metal · chains A, B

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

Pockets

13 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	811	0.79	0.83	90	empty
2	113	0.53	0.82	18	empty
3	66	0.53	0.86	16	empty
4	288	0.51	0.74	48	empty
5	229	0.50	0.75	28	empty

Interfaces

1 interface between chains.

A–B · 1896 Å² buried · 31 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 modified (engineered).

Compared structures

1TXK · Crystal structure of Escherichia coli OpgG · the same entry in another collection · chain A against A, TM-score 1.00
P33136 · AlphaFold monomer V2.0 prediction for glucans biosynthesis protein G (P33136) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 P33136
Elsewhere: RCSB PDB 1TXK · PDBe 1TXK · UniProt P33136

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