MolNFT v1 · #71687 · protein
Reduced (cu+) peptidylglycine alpha-hydroxylating monooxygenase (phm) with bound azide
3MLL · Peptidyl-glycine alpha-amidating monooxygenase: “Reduced (cu+) peptidylglycine alpha-hydroxylating monooxygenase (phm) with bound azide”. X-ray diffraction, 3 ligands (CU, NI, AZI), 3 pockets (best druggability 0.64). MolNFT v1…
- PDB
- 3MLL
- Type
- protein
- Length
- 304 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
- UniProt
- P14925
- Ligands
- CU, NI, AZI
- Pockets
- 3 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-glycine alpha-amidating monooxygenase (EC 1.14.17.3) | protein | 304 | 5% helix, 50% strand | P14925 |
Ligands and binding sites
- CU · Copper (II) ion · metal · chains A
- NI · Nickel (II) ion · metal · chains A
- AZI · Azide ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 493 | 0.64 | 0.77 | 43 | CU, AZI |
| 2 | 75 | 0.58 | 0.88 | 18 | empty |
| 3 | 59 | 0.48 | 0.85 | 17 | empty |
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 3MLL · Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound azide · 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 3MLL · PDBe 3MLL · UniProt P14925
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