Research workbench
X-ray reduced catalase 3 from N.CRASSA in cpd I state (0.135 mgy)
Analyse X-ray reduced catalase 3 from N.CRASSA in cpd I state (0.135 mgy) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NSW
- Type
- protein
- Length
- 2,715 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9C169
- Ligands
- HEM, O
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 682 | — | Q9C169 |
| B | — | protein | 677 | — | Q9C169 |
| C | — | protein | 679 | — | Q9C169 |
| D | — | protein | 677 | — | Q9C169 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, D, B, C
- O · Oxygen atom · ion · 4 copies · chains A, B, C, D
- EDO · 1,2-ethanediol · additive · 10 copies · chains A, B, C, D
- ACT · Acetate ion · additive · 8 copies · chains A, B, C, D
- EOH · Ethanol · additive · 5 copies · chains A, B, D
- PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A, C
- PGE · Triethylene glycol · additive · 3 copies · chains A, B, D
- 1PE · Pentaethylene glycol · additive · chains B, C
- PG4 · Tetraethylene glycol · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 Q9C169
- Elsewhere: RCSB PDB 6NSW · PDBe 6NSW · UniProt Q9C169
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