MolNFT v1 · #39882 · protein
Allosteric inhibition of staphylococcus aureus D-ALANINE:D-alanine ligase revealed by crystallographic studies
2I87: “Allosteric inhibition of staphylococcus aureus D-ALANINE:D-alanine ligase revealed by crystallographic studies”. X-ray diffraction. MolNFT v1 #39882 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2I87
- Type
- protein
- Length
- 689 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q5HEB7
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 345 | — | Q5HEB7 |
| B | — | protein | 344 | — | Q5HEB7 |
Compared structures
- 2I87 · Allosteric inhibition of Staphylococcus aureus D-alanine:D-alanine ligase revealed by… · the same entry in another collection · chain A against A, TM-score 1.00
- Q5HEB7 · AlphaFold monomer V2.0 prediction for D-alanine--D-alanine ligase (Q5HEB7) · a predicted model of the same protein · chain B against A, TM-score 0.96
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 Q5HEB7
- Elsewhere: RCSB PDB 2I87 · PDBe 2I87 · UniProt Q5HEB7
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.