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Structure of deletion mutant of alpha-glucuronidase (TM0752) from thermotoga maritima

Analyse Structure of deletion mutant of alpha-glucuronidase (TM0752) from thermotoga… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BR4
Type: protein
Length: 468 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-glucosidase, putative
UniProt: Q9WZL1
Ligands: NAI, MN
Pockets: 1 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-glucosidase, putative	protein	468	47% helix, 15% strand	Q9WZL1

Ligands and binding sites

NAI · 1,4-dihydronicotinamide adenine dinucleotide · ligand · chains A
MN · Manganese (II) ion · metal · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	993	0.77	0.79	71	MN, NAI

Compared structures

7BR4 · Structure of deletion mutant of alpha-glucuronidase (TM0752) from Thermotoga maritima · 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 Q9WZL1
Elsewhere: RCSB PDB 7BR4 · PDBe 7BR4 · UniProt Q9WZL1

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