Research workbench
Crystal structure of H107A-peptidylglycine alpha-hydroxylating monooxygenase (phm) mutant (no cuh bound)
Analyse Crystal structure of H107A-peptidylglycine alpha-hydroxylating monooxygenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ALV
- Type
- protein
- Length
- 305 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-glycine alpha-amidating monooxygenase
- EC
- 1.14.17.3, 4.3.2.5
- UniProt
- P14925
- Ligands
- CU, AZI
- Pockets
- 5 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-glycine alpha-amidating monooxygenase (EC 1.14.17.3, 4.3.2.5) | protein | 305 | 2% helix, 47% strand | P14925 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 2 copies · chains A
- AZI · Azide ion · ion · chains A
- GOL · Glycerol · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 462 | 0.61 | 0.75 | 48 | CU |
| 2 | 62 | 0.51 | 0.85 | 19 | GOL |
| 3 | 76 | 0.50 | 0.84 | 21 | GOL |
| 4 | 64 | 0.37 | 0.79 | 15 | empty |
| 5 | 50 | 0.28 | 0.75 | 14 | empty |
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 6ALV · Crystal structure of H107A-peptidylglycine alpha-hydroxylating monooxygenase (PHM) mutant… · the same entry in another collection · chain A against A, TM-score 1.00
- P14925 · AlphaFold monomer V2.0 prediction for peptidylglycine alpha-amidating monooxygenase… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P14925
- Elsewhere: RCSB PDB 6ALV · PDBe 6ALV · UniProt P14925
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.