Research workbench

Structure of thermomonospora curvata heme-containing dyp-type peroxidase with a modified axial ligand

Analyse Structure of thermomonospora curvata heme-containing dyp-type peroxidase with a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7RMU
Type: protein
Length: 361 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dyp-type peroxidase
UniProt: D1A807
Ligands: HEM, SO4
Pockets: 4 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dyp-type peroxidase	protein	361	27% helix, 22% strand	D1A807

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
SO4 · Sulfate ion · ion · 7 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	400	0.84	0.92	49	HEM
2	261	0.59	0.79	36	empty
3	92	0.46	0.80	22	empty
4	58	0.29	0.75	19	empty

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

7RMU · Structure of Thermomonospora curvata heme-containing DyP-type peroxidase with a modified… · 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 D1A807
Elsewhere: RCSB PDB 7RMU · PDBe 7RMU · UniProt D1A807

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