MolNFT v1 · #17085 · protein
Cohesin-dockerin complex from the cellulosome of clostridium thermocellum
1OHZ · Cellulosomal scaffolding protein a: “Cohesin-dockerin complex from the cellulosome of clostridium thermocellum”. X-ray diffraction, 3 ligands (CA, NO3, CL). MolNFT v1 #17085 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1OHZ
- Type
- protein
- Length
- 196 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellulosomal scaffolding protein a; Endo-1,4-beta-xylanase Y
- EC
- 3.2.1.8
- UniProt
- Q06851, P51584
- Ligands
- CA, NO3, CL
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cellulosomal scaffolding protein a | protein | 140 | 3% helix, 54% strand | Q06851 |
| B | Endo-1,4-beta-xylanase Y (EC 3.2.1.8) | protein | 56 | 52% helix, 0% strand | P51584 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains B
- NO3 · Nitrate ion · ion · 2 copies · chains A
- CL · Chloride ion · ion · chains B
- EDO · 1,2-ethanediol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 789 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 1OHZ · Cohesin-Dockerin complex from the cellulosome of Clostridium thermocellum · the same entry in another collection · chain A against A, TM-score 1.00
- Q06851 · AlphaFold monomer V2.0 prediction for cellulosomal-scaffolding protein a (Q06851) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P51584 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase Y (P51584) · a predicted model of the same protein · chain B 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 Q06851
- Every structure of UniProt P51584
- Elsewhere: RCSB PDB 1OHZ · PDBe 1OHZ · UniProt Q06851 · UniProt P51584
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