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Crystal structure of the arginine-bound form of domain 1 from tmargbp

Analyse Crystal structure of the arginine-bound form of domain 1 from tmargbp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6GPC
Type: protein
Length: 252 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amino acid ABC transporter, periplasmic amino acid-binding PROTEIN,AMINO acid ABC…
UniProt: Q9WZ62
Ligands: ARG
Pockets: 2 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Amino acid ABC transporter, periplasmic amino acid-binding PROTEIN,AMINO acid ABC transporter, periplasmic amino acid-binding protein	protein	126	36% helix, 23% strand	Q9WZ62

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

2 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	52	0.29	0.76	16	ARG
2	50	0.25	0.72	8	empty

Interfaces

1 interface between chains.

A–B · 485 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6GPC · Crystal structure of the arginine-bound form of domain 1 from TmArgBP · 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 Q9WZ62
Elsewhere: RCSB PDB 6GPC · PDBe 6GPC · UniProt Q9WZ62

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