Research workbench

Crystal structure of the binary complex of agre C264A mutant with L- arginine

Analyse Crystal structure of the binary complex of agre C264A mutant with L- arginine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6LRH
Type: protein
Length: 1,339 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ALR4995 protein
UniProt: Q8YMD9
Ligands: ARG
Pockets: 19 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ALR4995 protein	protein	675	34% helix, 23% strand	Q8YMD9
B	ALR4995 protein	protein	664	34% helix, 23% strand	Q8YMD9

Ligands and binding sites

ARG · Arginine · ligand · 2 copies · chains A, B

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

Pockets

19 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	143	0.78	0.95	28	empty
2	79	0.76	0.98	19	empty
3	59	0.71	0.97	22	empty
4	499	0.67	0.78	48	empty
5	329	0.64	0.80	33	empty

Interfaces

1 interface between chains.

A–B · 1204 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

6LRH · Crystal Structure of the Binary Complex of AgrE C264A mutant with L-arginine · the same entry in another collection · chain B against B, 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 Q8YMD9
Elsewhere: RCSB PDB 6LRH · PDBe 6LRH · UniProt Q8YMD9

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.