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Single-particle cryo-EM structure of arabinofuranosyltransferase aftd from mycobacteria, mutant R1389S class 1

Analyse Single-particle cryo-EM structure of arabinofuranosyltransferase aftd from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6WBX
Type: protein
Length: 1,264 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DUF3367 domain-containing protein
UniProt: A0A418KZ72
Ligands: CA
Pockets: 18 · best druggability 0.80

Structure

electron microscopy · 1 distinct chain · 25% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DUF3367 domain-containing protein	protein	1264	25% helix, 20% strand	A0A418KZ72

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A

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

Pockets

18 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	449	0.80	0.88	61	empty
2	896	0.80	0.82	125	empty
3	146	0.78	0.95	31	empty
4	833	0.76	0.80	93	empty
5	62	0.69	0.97	22	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

6WBX · Single-Particle Cryo-EM Structure of Arabinofuranosyltransferase AftD from Mycobacteria… · 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 A0A418KZ72
Elsewhere: RCSB PDB 6WBX · PDBe 6WBX · UniProt A0A418KZ72

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