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Structure of arg-bound escherichia COLI adic

Analyse Structure of arg-bound escherichia COLI adic in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3L1L
Type: protein
Length: 423 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ARGININE/AGMATINE antiporter
UniProt: P60063
Ligands: ARG, BNG
Pockets: 6 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 74% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ARGININE/AGMATINE antiporter	protein	423	74% helix, 0% strand	P60063

Ligands and binding sites

ARG · Arginine · ligand · chains A
BNG · nonyl beta-D-glucopyranoside · ligand · chains A

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

Pockets

6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	216	0.48	0.74	37	empty
2	53	0.41	0.82	21	empty
3	77	0.40	0.77	13	empty
4	76	0.34	0.74	12	empty
5	73	0.30	0.72	16	empty

Compared structures

3L1L · Structure of Arg-bound Escherichia coli AdiC · the same entry in another collection · chain A against A, TM-score 1.00
P60063 · AlphaFold monomer V2.0 prediction for ARGININE/AGMATINE antiporter (P60063) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P60063
Elsewhere: RCSB PDB 3L1L · PDBe 3L1L · UniProt P60063

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