Research workbench

Structure of D-carbamoylase from nitratireductor indicus

Analyse Structure of D-carbamoylase 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: 6LEI
Type: protein
Length: 611 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-carbamoyl-D-amino-acid hydrolase
UniProt: K2NMS4
Pockets: 2 · best druggability 0.75

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-carbamoyl-D-amino-acid hydrolase	protein	304	29% helix, 27% strand	K2NMS4
B	N-carbamoyl-D-amino-acid hydrolase	protein	307	30% helix, 28% strand	K2NMS4

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 5 copies · chains B, 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	258	0.75	0.89	35	empty
2	384	0.68	0.81	33	EDO

Interfaces

1 interface between chains.

A–B · 2799 Å² buried · 31 hydrogen bonds · protein-protein

Compared structures

6LEI · Structure of D-carbamoylase 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 6LEI · PDBe 6LEI · UniProt K2NMS4

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.