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Crystal structure of E. COLI lsrg

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

PDB: 3QMQ
Type: protein
Length: 392 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Autoinducer-2 (ai-2) modifying protein lsrg
UniProt: D3QT67
Pockets: 3 · best druggability 0.77

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Autoinducer-2 (ai-2) modifying protein lsrg	protein	97	39% helix, 37% strand	D3QT67
C, D	Autoinducer-2 (ai-2) modifying protein lsrg	protein	99	35% helix, 36% strand	D3QT67

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	559	0.77	0.84	67	empty
2	79	0.61	0.89	21	empty
3	68	0.59	0.89	20	empty

Interfaces

5 interfaces between chains.

B–C · 1177 Å² buried · 21 hydrogen bonds · protein-protein
A–D · 1169 Å² buried · 21 hydrogen bonds · protein-protein
A–B · 375 Å² buried · 4 hydrogen bonds · protein-protein
C–D · 114 Å² buried · 0 hydrogen bonds · protein-protein
B–D · 18 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

3QMQ · Crystal Structure of E. coli LsrG · 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 D3QT67
Elsewhere: RCSB PDB 3QMQ · PDBe 3QMQ · UniProt D3QT67

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