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Granulibacter bethesdensis allophanate hydrolase apo

Analyse Granulibacter bethesdensis allophanate hydrolase apo in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4GYR
Type
protein
Length
922 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Allophanate hydrolase
EC
3.5.1.54
UniProt
Q0BRB0
Pockets
7 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAllophanate hydrolase (EC 3.5.1.54)protein46137% helix, 17% strandQ0BRB0

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15540.690.7953empty
22570.600.8034empty
3930.450.8019empty
41040.440.7922empty
51100.440.7825empty

Interfaces

1 interface between chains.

  • A–B · 901 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 4GYR · Granulibacter bethesdensis allophanate hydrolase apo · the same entry in another collection · chain A against A, TM-score 1.00

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