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Inter-subunit signaling in gsam

Analyse Inter-subunit signaling in gsam in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2HP2
Type: protein
Length: 854 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamate-1-semialdehyde 2,1-aminomutase (gsam) hybrid- form
EC: 5.4.3.8
UniProt: P24630
Ligands: KE4, PLP, HOZ
Pockets: 5 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glutamate-1-semialdehyde 2,1-aminomutase (gsam) hybrid- form (EC 5.4.3.8)	protein	427	42% helix, 17% strand	P24630

Ligands and binding sites

KE4 · (4R)-5-amino-4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]pentanoic acid · ligand · chains A, B
PLP · Pyridoxal-5'-phosphate · ligand · chains A, B
HOZ · (4S)-4,5-diaminopentanoic acid · ligand · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	147	0.80	0.97	33	PLP, HOZ
2	72	0.77	0.99	21	empty
3	74	0.76	0.99	22	empty
4	663	0.75	0.81	69	KE4
5	56	0.32	0.77	15	empty

Interfaces

1 interface between chains.

A–B · 4698 Å² buried · 59 hydrogen bonds · protein-protein

Modifications

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

Compared structures

2HP2 · Inter-subunit signaling in 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 B against A, TM-score 0.99

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 2HP2 · PDBe 2HP2 · UniProt P24630

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