Research workbench
Crystal structure of the nucleotide binding domain fbpc complexed with ATP
Analyse Crystal structure of the nucleotide binding domain fbpc complexed with ATP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FVQ
- Type
- protein
- Length
- 693 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q5FA19
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 343 | — | Q5FA19 |
| B | — | protein | 350 | — | Q5FA19 |
Compared structures
- 3FVQ · Crystal structure of the nucleotide binding domain FbpC complexed with ATP · the same entry in another collection · chain A against A, TM-score 1.00
- Q5FA19 · AlphaFold monomer V2.0 prediction for FE(3+) ions import ATP-binding protein fbpc (Q5FA19) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q5FA19
- Elsewhere: RCSB PDB 3FVQ · PDBe 3FVQ · UniProt Q5FA19
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