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Structure of phosphonate hydroxylase

Analyse Structure of phosphonate hydroxylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5EQN
Type: protein
Length: 539 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Frbj
UniProt: Q0ZQ39
Ligands: MG
Pockets: 6 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Frbj	protein	270	37% helix, 23% strand	Q0ZQ39
B	Frbj	protein	269	38% helix, 22% strand	Q0ZQ39

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	234	0.57	0.78	31	MG
2	247	0.57	0.78	31	MG
3	126	0.40	0.74	25	empty
4	94	0.37	0.76	22	empty
5	97	0.34	0.73	24	empty

Interfaces

1 interface between chains.

A–B · 959 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

5EQN · Structure of phosphonate hydroxylase · the same entry in another collection · chain A against A, 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 Q0ZQ39
Elsewhere: RCSB PDB 5EQN · PDBe 5EQN · UniProt Q0ZQ39

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