GL1X · GenesisL1 explorer

Research workbench

Crystal structure of catalytic domain of anhydrobiosis-related mn- dependent peroxidase (amnp) from ramazzottius varieornatus (ZN2+- bound form)

Analyse Crystal structure of catalytic domain of anhydrobiosis-related mn- dependent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7DBU
Type
protein
Length
319 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
AMNP/G12777
UniProt
A0A1D1VPD8
Ligands
ZN
Pockets
1 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 45% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAMNP/G12777protein1617% helix, 45% strandA0A1D1VPD8
BAMNP/G12777protein1588% helix, 46% strandA0A1D1VPD8

Ligands and binding sites

  • ZN · Zinc ion · metal · 11 copies · chains A, B

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
12760.570.7748ZN

Interfaces

1 interface between chains.

  • A–B · 347 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 7DBU · Crystal structure of catalytic domain of Anhydrobiosis-related Mn-dependent Peroxidase… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.