MolNFT v1 · #159817 · protein
Crystal structure of mtb aspartate decarboxylase mutant M117I
6P1Y · Aspartate 1-decarboxylase beta chain: “Crystal structure of mtb aspartate decarboxylase mutant M117I”. X-ray diffraction, 2 ligands (PYR, NH4). MolNFT v1 #159817 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6P1Y
- Type
- protein
- Length
- 125 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate 1-decarboxylase beta chain; Aspartate 1-decarboxylase alpha chain
- EC
- 4.1.1.11
- UniProt
- P9WIL3
- Ligands
- PYR, NH4
Structure
x-ray diffraction · 2 distinct chains · 14% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate 1-decarboxylase beta chain (EC 4.1.1.11) | protein | 24 | 0% helix, 67% strand | P9WIL3 |
| B | Aspartate 1-decarboxylase alpha chain (EC 4.1.1.11) | protein | 101 | 17% helix, 42% strand | P9WIL3 |
Ligands and binding sites
- PYR · Pyruvic acid · ligand · chains B
- NH4 · Ammonium ion · ion · chains A
- TLA · L(+)-tartaric acid · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1744 Ų buried · 41 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
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 P9WIL3
- Elsewhere: RCSB PDB 6P1Y · PDBe 6P1Y · UniProt P9WIL3
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