MolNFT v1 · #157258 · protein

E. COLI DHFR complex modeled with three ligand states

6MTH · Dihydrofolate reductase: “E. COLI DHFR complex modeled with three ligand states”. X-ray diffraction, 3 ligands (DHF, MG, CL). MolNFT v1 #157258 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6MTH
Type: protein
Length: 161 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrofolate reductase
EC: 1.5.1.3
UniProt: P0ABQ4
Ligands: DHF, MG, CL

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrofolate reductase (EC 1.5.1.3)	protein	161	26% helix, 30% strand	P0ABQ4

Ligands and binding sites

DHF · Dihydrofolic acid · ligand · chains A
MG · Magnesium ion · metal · 4 copies · chains A
CL · Chloride ion · ion · 3 copies · chains A

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

Modifications

Observed in the structure: 2 covalent, 2 modified (covalent ligand, nonstandard).

Compared structures

6MTH · E. coli DHFR complex modeled with three ligand states · the same entry in another collection · chain A against A, TM-score 1.00
P0ABQ4 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase (P0ABQ4) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P0ABQ4
Elsewhere: RCSB PDB 6MTH · PDBe 6MTH · UniProt P0ABQ4

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