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Structure of the arginine-bound form of truncated (residues 20-233) argbp from T. maritima

Analyse Structure of the arginine-bound form of truncated (residues 20-233) argbp from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6GGV
Type
protein
Length
425 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
UniProt
Q9WZ62
Ligands
ARG, CD
Pockets
2 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAmino acid ABC transporter, periplasmic amino acid-binding proteinprotein21235% helix, 26% strandQ9WZ62
BAmino acid ABC transporter, periplasmic amino acid-binding proteinprotein21335% helix, 26% strandQ9WZ62

Ligands and binding sites

  • ARG · Arginine · ligand · 2 copies · chains A, B
  • CD · Cadmium ion · metal · 22 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12140.600.8132empty
23570.600.7727empty

Interfaces

1 interface between chains.

  • A–B · 644 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 6GGV · Structure of the arginine-bound form of truncated (residues 20-233) ArgBP from T. maritima · the same entry in another collection · chain A against A, TM-score 1.00

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