MolNFT v1 · #5291 · protein
Single crystal structure determination of the catalytic domain of celcca carried out at 15 degree C
1EDG: “Single crystal structure determination of the catalytic domain of celcca carried out at 15 degree C”. X-ray diffraction. MolNFT v1 #5291 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1EDG
- Type
- protein
- Length
- 380 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P17901
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 380 | — | P17901 |
Compared structures
- 1EDG · Single crystal structure determination of the catalytic domain of celcca carried out at… · the same entry in another collection · chain A against A, TM-score 1.00
- P17901 · AlphaFold monomer V2.0 prediction for endoglucanase a (P17901) · a predicted model of the same protein · 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 P17901
- Elsewhere: RCSB PDB 1EDG · PDBe 1EDG · UniProt P17901
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