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Ddah from pseudomonas aeruginosa. C249S mutant complexed with citrulline

Analyse Ddah from pseudomonas aeruginosa. C249S mutant complexed with citrulline in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1H70
Type: protein
Length: 255 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ng, ng-dimethylarginine dimethylaminohydrolase
EC: 3.5.3.18
UniProt: Q9I4E3
Ligands: CIR
Pockets: 2 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ng, ng-dimethylarginine dimethylaminohydrolase (EC 3.5.3.18)	protein	255	31% helix, 25% strand	Q9I4E3

Ligands and binding sites

CIR · Citrulline · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	134	0.80	0.98	26	empty
2	166	0.58	0.82	32	CIR

Compared structures

1H70 · Ddah from pseudomonas aeruginosa. C249S mutant complexed with citrulline · the same entry in another collection · chain A against A, TM-score 1.00
Q9I4E3 · AlphaFold monomer V2.0 prediction for N(G),N(G)-dimethylarginine dimethylaminohydrolase… · 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 Q9I4E3
Elsewhere: RCSB PDB 1H70 · PDBe 1H70 · UniProt Q9I4E3

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