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Pamurf in complex with AMP-pnp

Analyse Pamurf in complex with AMP-pnp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4CVL
Type
protein
Length
426 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Udp-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
EC
6.3.2.10
UniProt
Q9HVZ7
Ligands
ACP, MG
Pockets
1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUdp-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase (EC 6.3.2.10)protein42637% helix, 22% strandQ9HVZ7

Ligands and binding sites

  • ACP · Phosphomethylphosphonic acid adenylate ester · ligand · chains A
  • MG · Magnesium ion · metal · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13090.560.7633ACP

Compared structures

  • 4CVL · PaMurF in complex with AMP-PNP · the same entry in another collection · chain A against A, TM-score 1.00

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