MolNFT v2 · #156618 · protein
Structure of D-carbamoylase mutant from Nitratireductor indicus
6LCG: “Structure of D-carbamoylase mutant from Nitratireductor indicus”. X-ray diffraction at 2.7. MolNFT v2 #156618 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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
- UniProt
- K2NMS4
Structure
x-ray diffraction · resolution 2.7 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 303 | — | K2NMS4 |
| B | — | protein | 301 | — | 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.
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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