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Crystal structure of apo wild type peptidylglycine alpha-hydroxylating monooxygenase (phm) soaked with peptide (peptide not observed)

Analyse Crystal structure of apo wild type peptidylglycine alpha-hydroxylating… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5WM0
Type: protein
Length: 309 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
Pockets: 2 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 6% 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	309	6% helix, 47% strand	P14925

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	366	0.57	0.75	42	empty
2	67	0.31	0.75	17	empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

5WM0 · Crystal structure of apo wild type peptidylglycine alpha-hydroxylating monooxygenase… · 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 0.97

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 P14925
Elsewhere: RCSB PDB 5WM0 · PDBe 5WM0 · UniProt P14925

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