MolNFT v1 · #5030 · protein

Proline 3-hydroxylase (type II) -apo form

1E5R · Proline oxidase: “Proline 3-hydroxylase (type II) -apo form”. X-ray diffraction, 4 pockets (best druggability 0.66). MolNFT v1 #5030 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1E5R
Type: protein
Length: 522 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proline oxidase
UniProt: O09345
Pockets: 4 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Proline oxidase	protein	260	32% helix, 25% strand	O09345
B	Proline oxidase	protein	262	31% helix, 25% strand	O09345

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	523	0.66	0.77	61	empty
2	247	0.63	0.81	36	empty
3	174	0.58	0.81	33	empty
4	69	0.32	0.75	17	empty

Interfaces

1 interface between chains.

A–B · 420 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

1E5R · Proline 3-hydroxylase (type II) -apo form · the same entry in another collection · chain A against A, TM-score 1.00
O09345 · AlphaFold monomer V2.0 prediction for L-proline cis-3-hydroxylase 2 (O09345) · a predicted model of the same protein · chain B against A, TM-score 0.96

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 O09345
Elsewhere: RCSB PDB 1E5R · PDBe 1E5R · UniProt O09345

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