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Crystal structure of the first R-stereoselective -transaminase identified from arthrobacter sp. KNK168 (ferm-bp-5228)

Analyse Crystal structure of the first R-stereoselective -transaminase identified from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WWH
Type: protein
Length: 329 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: (R)-amine transaminase
EC: 2.6.1.18
UniProt: F7J696
Ligands: PLP
Pockets: 3 · best druggability 0.66

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	(R)-amine transaminase (EC 2.6.1.18)	protein	329	27% helix, 27% strand	F7J696

Ligands and binding sites

PLP · Pyridoxal-5'-phosphate · ligand · chains A
GOL · Glycerol · additive · chains A

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

Pockets

3 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	172	0.66	0.86	33	PLP, GOL
2	147	0.44	0.75	24	empty
3	70	0.30	0.73	18	empty

Modifications

Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).

Compared structures

3WWH · Crystal structure of the first R-stereoselective -transaminase identified from… · 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 F7J696
Elsewhere: RCSB PDB 3WWH · PDBe 3WWH · UniProt F7J696

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