Research workbench
Cooperativity in ef-hand CA2+-binding proteins: evidence of site-site communication from binding-induced changes in structure and dynamics of N56A calbindin D9K
Analyse Cooperativity in ef-hand CA2+-binding proteins: evidence of site-site… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1D1O
- Type
- protein
- Length
- 75 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calbindin D9K
- UniProt
- P02633
Structure
solution nmr · 1 distinct chain · 64% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calbindin D9K | protein | 75 | 64% helix, 8% strand | P02633 |
Compared structures
- 1D1O · Cooperativity in ef-hand CA2+-binding proteins: evidence of site-site communication from… · the same entry in another collection · chain A against A, TM-score 1.00
- P02633 · AlphaFold monomer V2.0 prediction for protein S100-G (P02633) · a predicted model of the same protein · chain A against A, TM-score 0.86
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 P02633
- Elsewhere: RCSB PDB 1D1O · PDBe 1D1O · UniProt P02633
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