MolNFT v1 · #96265 · protein
Different contribution of conserved amino acids to the global properties of homologous enzymes
4JEQ: “Different contribution of conserved amino acids to the global properties of homologous enzymes”. X-ray diffraction. MolNFT v1 #96265 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4JEQ
- Type
- protein
- Length
- 2,968 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04789
Structure
x-ray diffraction · 9 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, E | — | protein | 250 | — | P04789 |
| B | — | protein | 245 | — | P04789 |
| C | — | protein | 248 | — | P04789 |
| F, J | — | protein | 249 | — | P04789 |
| G | — | protein | 245 | — | P04789 |
| H | — | protein | 243 | — | P04789 |
| I | — | protein | 247 | — | P04789 |
| K | — | protein | 246 | — | P04789 |
| L | — | protein | 246 | — | P04789 |
Compared structures
- 4JEQ · Different Contribution of Conserved Amino Acids to the Global Properties of Homologous… · the same entry in another collection · chain J against J, 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 P04789
- Elsewhere: RCSB PDB 4JEQ · PDBe 4JEQ · UniProt P04789
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