MolNFT v1 · #120043 · protein
Structure of deg protease hhoa from synechocystis sp. pcc 6803
5GND · Putative serine protease hhoa: “Structure of deg protease hhoa from synechocystis sp. pcc 6803”. X-ray diffraction, 2 ligands (ZN, NA), 1 pocket (best druggability 0.40). MolNFT v1 #120043 on GenesisL1: 3D structure, binding sites…
- PDB
- 5GND
- Type
- protein
- Length
- 285 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative serine protease hhoa; Unk-unk-unk-unk-TRP
- UniProt
- P72780
- Ligands
- ZN, NA
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 15% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative serine protease hhoa | protein | 280 | 16% helix, 36% strand | P72780 |
| U | Unk-unk-unk-unk-TRP | protein | 5 | 0% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 143 | 0.40 | 0.73 | 29 | empty |
Interfaces
1 interface between chains.
- A–U · 358 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 5GND · Structure of Deg protease HhoA from Synechocystis sp. PCC 6803 · the same entry in another collection · chain A against A, TM-score 1.00
- P72780 · AlphaFold monomer V2.0 prediction for putative serine protease hhoa (P72780) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P72780
- Elsewhere: RCSB PDB 5GND · PDBe 5GND · UniProt P72780
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