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Opha DELTAC6 V404F complex with sah

Analyse Opha DELTAC6 V404F complex with sah in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6R00
Type: protein
Length: 398 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptide N-methyltransferase; Phe-pro-TRP-mva-ile-mva-phe-gly-val-ile-gly-val-ile-gly
UniProt: A0A2R2JFI5
Ligands: SAH
Pockets: 2 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptide N-methyltransferase	protein	384	40% helix, 15% strand	A0A2R2JFI5
B	Phe-pro-TRP-mva-ile-mva-phe-gly-val-ile-gly-val-ile-gly	protein	14	0% helix, 0% strand	—

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	124	0.80	0.97	31	SAH
2	140	0.47	0.77	18	empty

Interfaces

1 interface between chains.

A–B · 1067 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (methylation).

Compared structures

6R00 · OphA DeltaC6 V404F complex with SAH · 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 A0A2R2JFI5
Elsewhere: RCSB PDB 6R00 · PDBe 6R00 · UniProt A0A2R2JFI5

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