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Crystal structure of C171A/V236A mutant of N-carbamyl-D-amino acid amidohydrolase

Analyse Crystal structure of C171A/V236A mutant of N-carbamyl-D-amino acid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1UF4
Type: protein
Length: 606 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-carbamyl-D-amino acid amidohydrolase
EC: 3.5.1.77
UniProt: P60327
Pockets: 3 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	N-carbamyl-D-amino acid amidohydrolase (EC 3.5.1.77)	protein	303	32% helix, 28% strand	P60327

Pockets

3 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	253	0.79	0.92	43	empty
2	295	0.79	0.91	46	empty
3	52	0.26	0.74	13	empty

Interfaces

1 interface between chains.

A–B · 2516 Å² buried · 27 hydrogen bonds · protein-protein

Compared structures

1UF4 · Crystal structure of C171A/V236A Mutant of N-carbamyl-D-amino acid amidohydrolase · the same entry in another collection · chain A against A, TM-score 1.00
P60327 · AlphaFold monomer V2.0 prediction for N-carbamoyl-D-amino acid hydrolase (P60327) · a predicted model of the same protein · chain B 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 P60327
Elsewhere: RCSB PDB 1UF4 · PDBe 1UF4 · UniProt P60327

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