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Solution NMR structure of the ob-fold domain of heme chaperone ccme from desulfovibrio vulgaris. northeast structural genomics target DVR115G.
Analyse Solution NMR structure of the ob-fold domain of heme chaperone ccme from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KCT
- Type
- protein
- Length
- 88 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C-type biogenesis protein ccme
- UniProt
- Q72D78
Structure
solution nmr · 1 distinct chain · 0% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C-type biogenesis protein ccme | protein | 88 | 0% helix, 45% strand | Q72D78 |
Compared structures
- 2KCT · Solution nmr structure of the ob-fold domain of heme chaperone ccme from desulfovibrio… · the same entry in another collection · 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 Q72D78
- Elsewhere: RCSB PDB 2KCT · PDBe 2KCT · UniProt Q72D78
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