MolNFT v1 · #144720 · protein

The molecular basis for the functional evolution of an organophosphate hydrolysing enzyme

6C2C · Dihydrocoumarin hydrolase, ANCDHCH1: “The molecular basis for the functional evolution of an organophosphate hydrolysing enzyme”. X-ray diffraction, 2 ligands (ZN, MG), 5 pockets (best druggability 0.86). MolNFT v1 #144720 on…

PDB: 6C2C
Type: protein
Length: 598 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrocoumarin hydrolase, ANCDHCH1
Ligands: ZN, MG
Pockets: 5 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Dihydrocoumarin hydrolase, ANCDHCH1	protein	299	28% helix, 29% strand	—

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B
PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B

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

Pockets

5 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	1105	0.86	0.86	109	empty
2	52	0.59	0.91	16	PEG
3	50	0.37	0.80	16	empty
4	52	0.35	0.79	16	empty
5	63	0.32	0.75	15	empty

Interfaces

1 interface between chains.

A–B · 2361 Å² buried · 42 hydrogen bonds · protein-protein

Compared structures

6C2C · The molecular basis for the functional evolution of an organophosphate hydrolysing enzyme · 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
Elsewhere: RCSB PDB 6C2C · PDBe 6C2C

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