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Crystal structure of TM1643

Analyse Crystal structure of TM1643 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1H2H
Type: protein
Length: 233 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein TM1643
UniProt: Q9X1X6
Ligands: NAD
Pockets: 2 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein TM1643	protein	233	37% helix, 25% strand	Q9X1X6

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A

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

Pockets

2 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	227	0.54	0.77	39	NAD
2	143	0.39	0.72	21	empty

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

1H2H · Crystal structure of TM1643 · the same entry in another collection · chain A against A, TM-score 1.00
Q9X1X6 · AlphaFold monomer V2.0 prediction for L-aspartate dehydrogenase (Q9X1X6) · a predicted model of the same protein · chain A 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 Q9X1X6
Elsewhere: RCSB PDB 1H2H · PDBe 1H2H · UniProt Q9X1X6

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