Research workbench
Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 ångströms resolution
Analyse Crystallographic refinement and atomic models of two different forms of citrate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CTS
- Type
- protein
- Length
- 437 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00889
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 437 | — | P00889 |
Compared structures
- 1CTS · Crystallographic refinement and atomic models of two different forms of citrate synthase… · the same entry in another collection · chain A against A, TM-score 1.00
- P00889 · AlphaFold monomer V2.0 prediction for citrate synthase, mitochondrial (P00889) · 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 P00889
- Elsewhere: RCSB PDB 1CTS · PDBe 1CTS · UniProt P00889
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