Research workbench
Crystal structure of the glutaryl-7-aminocephalosporanic acid acylase by mad phasing
Analyse Crystal structure of the glutaryl-7-aminocephalosporanic acid acylase by mad… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GHD
- Type
- protein
- Length
- 673 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutaryl-7-aminocephalosporanic acid acylase
- EC
- 3.5.1.-
- UniProt
- O86089
- Pockets
- 5 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutaryl-7-aminocephalosporanic acid acylase (EC 3.5.1.-) | protein | 153 | 65% helix, 5% strand | O86089 |
| B | Glutaryl-7-aminocephalosporanic acid acylase (EC 3.5.1.-) | protein | 520 | 25% helix, 29% strand | O86089 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 410 | 0.62 | 0.77 | 68 | empty |
| 2 | 93 | 0.42 | 0.78 | 19 | empty |
| 3 | 109 | 0.35 | 0.74 | 24 | empty |
| 4 | 68 | 0.32 | 0.75 | 13 | empty |
| 5 | 61 | 0.28 | 0.73 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 4065 Ų buried · 56 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 1GHD · Crystal structure of the glutaryl-7-aminocephalosporanic acid acylase by mad phasing · the same entry in another collection · chain B against B, TM-score 1.00
- 1GK0 · Structure-based prediction of modifications in glutarylamidase to allow single-step… · a predicted model of the same protein · chain B against D, TM-score 1.00
- 1GK1 · Structure-based prediction of modifications in glutarylamidase to allow single-step… · a predicted model of the same protein · chain B against D, 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 O86089
- Elsewhere: RCSB PDB 1GHD · PDBe 1GHD · UniProt O86089
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