MolNFT v1 · #70448 · protein
Tyrosine 447 of protocatechuate 3,4-dioxygenase controls efficient progress through catalysis
3LKT: “Tyrosine 447 of protocatechuate 3,4-dioxygenase controls efficient progress through catalysis”. X-ray diffraction. MolNFT v1 #70448 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3LKT
- Type
- protein
- Length
- 2,628 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00436, P00437
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | — | protein | 200 | — | P00436 |
| M, N, O, P, Q, R | — | protein | 238 | — | P00437 |
Compared structures
- 3LKT · Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through… · the same entry in another collection · chain R against R, 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 P00436
- Every structure of UniProt P00437
- Elsewhere: RCSB PDB 3LKT · PDBe 3LKT · UniProt P00436 · UniProt P00437
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