MolNFT v2 · #148986 · protein

Structure of E285D S. cerevisiae Fdc1 with prFMN in the hydroxylated form

6EVF: “Structure of E285D S. cerevisiae Fdc1 with prFMN in the hydroxylated form”. X-ray diffraction at 2.06, 3 ligands (4LU, MN, K). MolNFT v2 #148986 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6EVF
Type: protein
Length: 2,006 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.06
Source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
UniProt: Q03034
Ligands: 4LU, MN, K

Structure

x-ray diffraction · resolution 2.06 · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	503	—	Q03034
B	—	protein	502	—	Q03034
C	—	protein	500	—	Q03034
D	—	protein	501	—	Q03034

Ligands and binding sites

4LU · 1-deoxy-5-O-phosphono-1-(3,3,4,5-tetramethyl-9,11-dioxo-2,3,8,9,10,11-hexahydro-7H-quinolino[1,8-fg]pteridin-12-ium-7-yl)-D-ribitol · ligand · 4 copies · chains A, B, C, D
MN · Manganese (II) ion · metal · 4 copies · chains A, B, C, D
K · Potassium ion · metal · 4 copies · chains A, B, C, D

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

Compared structures

6EVF · Structure of E285D S. cerevisiae FDC1 with prfmn in the hydroxylated form · the same entry in another collection · chain D against D, TM-score 1.00
Q03034 · AlphaFold monomer V2.0 prediction for ferulic acid decarboxylase 1 (Q03034) · a predicted model of the same protein · chain B 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 Q03034
Elsewhere: RCSB PDB 6EVF · PDBe 6EVF · UniProt Q03034

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