Research workbench

The (R)-selective transaminase from nectria haematococca with inhibitor bound

Analyse The (R)-selective transaminase from nectria haematococca with inhibitor bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4CMF
Type: protein
Length: 322 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminotransferase
EC: 2.6.1.42
UniProt: C7YVL8
Ligands: PXG, SO4
Pockets: 2 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aminotransferase (EC 2.6.1.42)	protein	322	32% helix, 26% strand	C7YVL8

Ligands and binding sites

PXG · 3-[O-phosphonopyridoxyl]--amino-benzoic acid · ligand · chains A
SO4 · Sulfate ion · ion · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	176	0.66	0.86	31	PXG
2	113	0.40	0.75	18	empty

Compared structures

4CMF · The (R)-selective transaminase from Nectria haematococca with inhibitor bound · 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 C7YVL8
Elsewhere: RCSB PDB 4CMF · PDBe 4CMF · UniProt C7YVL8

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