Research workbench

M248I mutant of GSAM

Analyse M248I mutant of GSAM in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FQ8
Type: protein
Length: 854 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2
Source: Synechococcus elongatus PCC 6301
Molecule: Glutamate-1-semialdehyde 2,1-aminomutase
EC: 5.4.3.8
UniProt: P24630
Ligands: PMP
Pockets: 6 · best druggability 0.82

Structure

x-ray diffraction · resolution 2 · 1 distinct chain · 41% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glutamate-1-semialdehyde 2,1-aminomutase (EC 5.4.3.8)	protein	427	41% helix, 17% strand	P24630

Ligands and binding sites

PMP · 4'-deoxy-4'-aminopyridoxal-5'-phosphate · ligand · 2 copies · chains A, B

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

Pockets

6 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	162	0.82	0.97	39	PMP
2	149	0.81	0.97	37	PMP
3	66	0.76	0.99	21	empty
4	65	0.75	0.99	22	empty
5	50	0.70	0.98	19	empty

Interfaces

1 interface between chains.

A–B · 4685 Å² buried · 70 hydrogen bonds · protein-protein

Compared structures

3FQ8 · M248I mutant of gsam · the same entry in another collection · chain A against A, TM-score 1.00
P24630 · AlphaFold monomer V2.0 prediction for glutamate-1-semialdehyde 2,1-aminomutase (P24630) · a predicted model of the same protein · 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 P24630
Elsewhere: RCSB PDB 3FQ8 · PDBe 3FQ8 · UniProt P24630

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