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Crystal structure of apo L-rhamnonate dehydratase from escherichia COLI

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

PDB: 2I5Q
Type: protein
Length: 765 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L-rhamnonate dehydratase
UniProt: Q8XE07
Pockets: 6 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	L-rhamnonate dehydratase	protein	381	37% helix, 18% strand	Q8XE07
B	L-rhamnonate dehydratase	protein	384	38% helix, 18% strand	Q8XE07

Pockets

6 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	782	0.75	0.80	58	empty
2	98	0.75	0.97	33	empty
3	701	0.71	0.77	48	empty
4	216	0.55	0.78	31	empty
5	204	0.54	0.78	30	empty

Interfaces

1 interface between chains.

A–B · 2360 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

2I5Q · Crystal structure of Apo L-rhamnonate dehydratase from Escherichia Coli · the same entry in another collection · chain A against A, TM-score 1.00
Q8XE07 · AlphaFold monomer V2.0 prediction for L-rhamnonate dehydratase (Q8XE07) · a predicted model of the same protein · 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 Q8XE07
Elsewhere: RCSB PDB 2I5Q · PDBe 2I5Q · UniProt Q8XE07

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