Research workbench
Crystal structure of thermotoga maritima S- adenosylmethionine decarboxylase
Analyse Crystal structure of thermotoga maritima S- adenosylmethionine decarboxylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TLU
- Type
- protein
- Length
- 234 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- S-adenosylmethionine decarboxylase proenzyme, adometdc, samdc
- EC
- 4.1.1.50
- UniProt
- Q9WZC3
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | S-adenosylmethionine decarboxylase proenzyme, adometdc, samdc (EC 4.1.1.50) | protein | 117 | 29% helix, 46% strand | Q9WZC3 |
Interfaces
1 interface between chains.
- A–B · 1518 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 1TLU · Crystal Structure of Thermotoga maritima S-adenosylmethionine decarboxylase · the same entry in another collection · chain A against A, TM-score 1.00
- Q9WZC3 · AlphaFold monomer V2.0 prediction for S-adenosylmethionine decarboxylase proenzyme… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9WZC3
- Elsewhere: RCSB PDB 1TLU · PDBe 1TLU · UniProt Q9WZC3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.