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Mannosyltransferase pcmangt from pyrobaculum calidifontis

Analyse Mannosyltransferase pcmangt from pyrobaculum calidifontis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6YV7
Type: protein
Length: 691 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycosyl transferase, family 2
UniProt: A3MTD6
Pockets: 8 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 53% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycosyl transferase, family 2	protein	346	54% helix, 12% strand	A3MTD6
B	Glycosyl transferase, family 2	protein	345	53% helix, 12% strand	A3MTD6

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	633	0.76	0.82	59	empty
2	623	0.70	0.78	56	empty
3	776	0.69	0.75	64	empty
4	693	0.68	0.75	71	empty
5	50	0.59	0.92	16	empty

Interfaces

1 interface between chains.

A–B · 955 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

6YV7 · Mannosyltransferase PcManGT from Pyrobaculum calidifontis · 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 A3MTD6
Elsewhere: RCSB PDB 6YV7 · PDBe 6YV7 · UniProt A3MTD6

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