MolNFT v1 · #176110 · protein

Crystal structure of catalytic domain of anhydrobiosis-related mn- dependent peroxidase (amnp) from ramazzottius varieornatus (MN2+- bound form)

7DBT · AMNP/G12777: “Crystal structure of catalytic domain of anhydrobiosis-related mn- dependent peroxidase (amnp) from…”. X-ray diffraction, 1 ligand (MN), 1 pocket (best druggability 0.42). MolNFT v1 #176110 on GenesisL1: 3D structure…

PDB: 7DBT
Type: protein
Length: 310 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: AMNP/G12777
UniProt: A0A1D1VPD8
Ligands: MN
Pockets: 1 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	AMNP/G12777	protein	155	6% helix, 48% strand	A0A1D1VPD8

Ligands and binding sites

MN · Manganese (II) ion · metal · 4 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	183	0.42	0.73	25	empty

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

7DBT · 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

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A0A1D1VPD8
Elsewhere: RCSB PDB 7DBT · PDBe 7DBT · UniProt A0A1D1VPD8

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