MolNFT v1 · #105333 · protein

Crystal structure of petunia hydrida cinnamoyl-CoA reductase

4R1S · Cinnamoyl CoA reductase: “Crystal structure of petunia hydrida cinnamoyl-CoA reductase”. X-ray diffraction, 1 ligand (NAP), 4 pockets (best druggability 0.78). MolNFT v1 #105333 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 4R1S
Type: protein
Length: 637 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cinnamoyl CoA reductase
Ligands: NAP
Pockets: 4 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cinnamoyl CoA reductase	protein	319	42% helix, 17% strand	—
B	Cinnamoyl CoA reductase	protein	318	42% helix, 16% strand	—

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B

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

Pockets

4 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	1041	0.78	0.80	77	NAP
2	991	0.78	0.80	77	NAP
3	73	0.38	0.78	17	empty
4	54	0.31	0.76	16	empty

Interfaces

1 interface between chains.

A–B · 852 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

4R1S · Crystal structure of Petunia hydrida cinnamoyl-CoA reductase · 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 4R1S · PDBe 4R1S

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