Research workbench
Pelc from geobacter metallireducens
Analyse Pelc from geobacter metallireducens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5T0Z
- Type
- protein
- Length
- 627 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipoprotein, putative
- UniProt
- Q39U79
- Pockets
- 14 · best druggability 0.88
Structure
x-ray diffraction · 4 distinct chains · 30% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipoprotein, putative | protein | 158 | 30% helix, 35% strand | Q39U79 |
| B | Lipoprotein, putative | protein | 158 | 30% helix, 34% strand | Q39U79 |
| C | Lipoprotein, putative | protein | 156 | 29% helix, 35% strand | Q39U79 |
| D | Lipoprotein, putative | protein | 155 | 30% helix, 35% strand | Q39U79 |
Pockets
14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 603 | 0.88 | 0.93 | 50 | empty |
| 2 | 634 | 0.88 | 0.93 | 52 | empty |
| 3 | 90 | 0.74 | 0.96 | 23 | empty |
| 4 | 147 | 0.68 | 0.89 | 28 | empty |
| 5 | 236 | 0.65 | 0.83 | 36 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1054 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 930 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 905 Ų buried · 21 hydrogen bonds · protein-protein
- A–D · 834 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 259 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 5T0Z · PelC from Geobacter metallireducens · 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 Q39U79
- Elsewhere: RCSB PDB 5T0Z · PDBe 5T0Z · UniProt Q39U79
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