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Crystal structure of apo E. COLI xylr

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

PDB: 4FE4
Type: protein
Length: 1,140 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Xylose operon regulatory protein
UniProt: P0ACI3
Pockets: 12 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Xylose operon regulatory protein	protein	380	44% helix, 12% strand	P0ACI3

Pockets

12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	859	0.77	0.81	70	empty
2	1200	0.77	0.79	93	empty
3	916	0.77	0.80	81	empty
4	940	0.77	0.80	85	empty
5	315	0.72	0.85	40	empty

Interfaces

2 interfaces between chains.

A–C · 2646 Å² buried · 28 hydrogen bonds · protein-protein
A–B · 427 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

4FE4 · Crystal structure of apo E. coli XylR · the same entry in another collection · chain A against A, TM-score 1.00
P0ACI3 · AlphaFold monomer V2.0 prediction for xylose operon regulatory protein (P0ACI3) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P0ACI3
Elsewhere: RCSB PDB 4FE4 · PDBe 4FE4 · UniProt P0ACI3

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