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Crystal structure of a phosphoserine aminotransferase serc (CHU_0995) from cytophaga hutchinsonii atcc 33406 at 1.75 a resolution

Analyse Crystal structure of a phosphoserine aminotransferase serc (CHU_0995) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FFR
Type: protein
Length: 361 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphoserine aminotransferase serc
EC: 2.6.1.52
UniProt: Q11WE4
Ligands: SER
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphoserine aminotransferase serc (EC 2.6.1.52)	protein	361	42% helix, 18% strand	Q11WE4

Ligands and binding sites

SER · Serine · ligand · chains A
P33 · 3,6,9,12,15,18-hexaoxaicosane-1,20-diol · additive · 11 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	62	0.36	0.78	18	empty

Modifications

Observed in the structure: 10 modified (engineered, cofactor).

Compared structures

3FFR · Crystal structure of a phosphoserine aminotransferase serc (CHU_0995) from cytophaga… · 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 Q11WE4
Elsewhere: RCSB PDB 3FFR · PDBe 3FFR · UniProt Q11WE4

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