MolNFT v1 · #34869 · protein
Thermodynamic and structural analyses of hydrolytic mechanism by catalytic antibodies
2DTM: “Thermodynamic and structural analyses of hydrolytic mechanism by catalytic antibodies”. X-ray diffraction. MolNFT v1 #34869 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2DTM
- Type
- protein
- Length
- 434 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A2NHM3, P18527
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | — | protein | 218 | — | A2NHM3 |
| H | — | protein | 216 | — | P18527 |
Compared structures
- 2DTM · Thermodynamic and structural analyses of hydrolytic mechanism by catalytic antibodies · the same entry in another collection · chain L against L, TM-score 1.00
- P18527 · AlphaFold monomer V2.0 prediction for ig heavy chain V region 914 (P18527) · a predicted model of the same protein · chain H against A, TM-score 0.44
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 A2NHM3
- Every structure of UniProt P18527
- Elsewhere: RCSB PDB 2DTM · PDBe 2DTM · UniProt A2NHM3 · UniProt P18527
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