MolNFT v1 · #39269 · protein

Inter-subunit signaling in gsam

2HOZ · Glutamate-1-semialdehyde 2,1-aminomutase (gsam) pmp-form: “Inter-subunit signaling in gsam”. X-ray diffraction, 2 ligands (PMP, HOZ), 5 pockets (best druggability 0.75). MolNFT v1 #39269 on GenesisL1: 3D structure, binding sites and…

PDB: 2HOZ
Type: protein
Length: 847 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamate-1-semialdehyde 2,1-aminomutase (gsam) pmp-form
EC: 5.4.3.8
UniProt: P24630
Ligands: PMP, HOZ
Pockets: 5 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutamate-1-semialdehyde 2,1-aminomutase (gsam) pmp-form (EC 5.4.3.8)	protein	427	41% helix, 18% strand	P24630
B	Glutamate-1-semialdehyde 2,1-aminomutase (gsam) pmp-form (EC 5.4.3.8)	protein	420	42% helix, 18% strand	P24630

Ligands and binding sites

PMP · 4'-deoxy-4'-aminopyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
HOZ · (4S)-4,5-diaminopentanoic acid · ligand · chains A

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	59	0.75	1.00	21	empty
2	606	0.75	0.81	61	PMP
3	562	0.73	0.81	56	PMP
4	54	0.34	0.77	16	empty
5	62	0.34	0.76	19	empty

Interfaces

1 interface between chains.

A–B · 4626 Å² buried · 66 hydrogen bonds · protein-protein

Compared structures

2HOZ · 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 2HOZ · PDBe 2HOZ · UniProt P24630

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