MolNFT v1 · #155590 · protein

Structure of D-carbamoylase mutant from nitratireductor indicus

6LCG · N-carbamoyl-D-amino-acid hydrolase: “Structure of D-carbamoylase mutant from nitratireductor indicus”. X-ray diffraction, 2 pockets (best druggability 0.69). MolNFT v1 #155590 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 6LCG
Type: protein
Length: 604 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 0.69

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	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 · 2760 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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