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Structure of D-carbamoylase mutant from Nitratireductor indicus

Analyse Structure of D-carbamoylase mutant from Nitratireductor indicus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6LCG
Type: protein
Length: 604 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.7
Source: Nitratireductor indicus C115
Molecule: N-carbamoyl-D-amino-acid hydrolase
UniProt: K2NMS4
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · resolution 2.7 · 2 distinct chains · 29% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-carbamoyl-D-amino-acid hydrolase	protein	303	29% helix, 28% strand	K2NMS4
B	N-carbamoyl-D-amino-acid hydrolase	protein	301	29% helix, 29% strand	K2NMS4

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B

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	422	0.69	0.81	41	empty
2	389	0.66	0.79	40	empty

Interfaces

1 interface between chains.

A–B · 2761 Å² buried · 29 hydrogen bonds · protein-protein

Compared structures

6LCG · Structure of D-carbamoylase mutant from nitratireductor indicus · the same entry in another collection · chain A 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 K2NMS4
Elsewhere: RCSB PDB 6LCG · PDBe 6LCG · UniProt K2NMS4

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