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Crystal structure of prochlorococcus marinus aldehyde-deformylating oxygenase wild type with palmitic acid bound

Analyse Crystal structure of prochlorococcus marinus aldehyde-deformylating oxygenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4KVQ
Type: protein
Length: 223 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aldehyde decarbonylase
EC: 4.1.99.5
UniProt: Q7V6D4
Ligands: PLM, FE
Pockets: 1 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 87% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aldehyde decarbonylase (EC 4.1.99.5)	protein	223	87% helix, 0% strand	Q7V6D4

Ligands and binding sites

PLM · Palmitic acid · ligand · chains A
FE · Fe (III) ion · metal · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	161	0.83	0.98	29	PLM

Compared structures

4KVQ · Crystal Structure of Prochlorococcus marinus aldehyde-deformylating oxygenase wild type… · the same entry in another collection · chain A against A, TM-score 1.00
Q7V6D4 · AlphaFold monomer V2.0 prediction for aldehyde decarbonylase (Q7V6D4) · 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 Q7V6D4
Elsewhere: RCSB PDB 4KVQ · PDBe 4KVQ · UniProt Q7V6D4

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