MolNFT v1 · #122006 · protein

Crystal structure of apo (S)-norcoclaurine 6-O-methyltransferase

5ICG: “Crystal structure of apo (S)-norcoclaurine 6-O-methyltransferase”. X-ray diffraction, 1 ligand (K), 1 pocket (best druggability 0.77). MolNFT v1 #122006 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5ICG
Type: protein
Length: 323 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: (S)-norcoclaurine 6-O-methyltransferase
EC: 2.1.1.128
UniProt: Q5C9L7
Ligands: K
Pockets: 1 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	(S)-norcoclaurine 6-O-methyltransferase (EC 2.1.1.128)	protein	323	52% helix, 16% strand	Q5C9L7

Ligands and binding sites

K · Potassium ion · metal · 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	973	0.77	0.79	68	empty

Compared structures

5ICG · Crystal structure of apo (S)-norcoclaurine 6-O-methyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
Q5C9L7 · AlphaFold monomer V2.0 prediction for (rs)-norcoclaurine 6-O-methyltransferase (Q5C9L7) · a predicted model of the same protein · chain A against A, TM-score 0.85

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 Q5C9L7
Elsewhere: RCSB PDB 5ICG · PDBe 5ICG · UniProt Q5C9L7

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