MolNFT v2 · #161968 · protein
Structure of CpGH84A
6PV4: “Structure of CpGH84A”. X-ray diffraction at 2.2, 1 ligand (CA). MolNFT v2 #161968 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6PV4
- Type
- protein
- Length
- 2,406 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.2
- Source
- Clostridium perfringens ATCC 13124
- UniProt
- A0A0H2YRL1
- Ligands
- CA
Structure
x-ray diffraction · resolution 2.2 · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 589 | — | A0A0H2YRL1 |
| B | — | protein | 607 | — | A0A0H2YRL1 |
| C | — | protein | 608 | — | A0A0H2YRL1 |
| D | — | protein | 602 | — | A0A0H2YRL1 |
Ligands and binding sites
- CA · Calcium ion · metal · 19 copies · chains A, B, C, D
- EDO · 1,2-ethanediol · additive · 23 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6PV4 · Structure of CPGH84A · 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 A0A0H2YRL1
- Elsewhere: RCSB PDB 6PV4 · PDBe 6PV4 · UniProt A0A0H2YRL1
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