› 4p68

X-ray diffraction
2.26Å resolution

Electrostatics of Active Site Microenvironments for E. coli DHFR

Released:
DOI: 10.2210/pdb4p68/pdb
PDB entry 4p68 coloured by chain, front view.
PDB entry 4p68 coloured by chain, side view.
PDB entry 4p68 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Probing the electrostatics of active site microenvironments along the catalytic cycle for Escherichia coli dihydrofolate reductase.
Liu CT, Layfield JP, Stewart RJ, French JB, Hanoian P, Asbury JB, Hammes-Schiffer S, Benkovic SJ
J Am Chem Soc 136 10349-60 (2014)
PMID: 24977791

Function and Biology Details

Reaction catalysed: 
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111221 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 17.99 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: C3TR70 (Residues: 1-159; Coverage: 100%)
Gene names: A5U30_000424, ACU57_16280, AW118_10375, AWP47_04925, B6R15_000347, B6R31_002587, BANRA_00523, BE932_23265, BER14_08425, BG944_001989, BGM66_001957, BJI68_09455, BK383_13950, BKL28_001204, BTB68_000362, BTQ06_18355, BXT93_23950, C0P57_001699, C1Q91_003816, C2121_001323, C2M16_10165, C2R31_000748, C9Z68_04175, CF22_002880, CG831_000939, CIG67_13370, CTR35_001675, D3C88_25840, D3G36_11580, D4N09_07475, D9D43_02920, D9E49_02790, D9J61_12405, DD762_00445, DIV22_05615, DNQ45_13535, DNX30_02935, DS732_05135, DTL43_06560, DU321_03045, E4K51_06405, E5H86_10110, E6D34_01590, ECs0051, EIA08_05700, EIMP300_82000, EIZ93_17180, EN85_002068, EPS76_03355, EWK56_14255, F7F11_02700, F7N46_19275, F9413_03865, F9461_05435, F9B07_04130, FGAF848_49820, FIJ20_19880, FJQ40_06615, FKO60_12985, FOI11_013455, FOI11_22225, FPI65_00190, FWK02_14090, FZU14_06390, G3V95_03040, G3W53_01145, G4A38_11125, G4A47_11355, G5603_15310, GAI89_10900, GAJ12_06545, GKF66_03125, GNW61_12025, GOP25_07845, GP711_08905, GP965_23705, GP965_31255, GP975_21565, GP975_31520, GP979_18430, GP979_24435, GQA06_14830, GQA06_14850, GQM04_06635, GQM04_12850, GQM21_07420, GQN34_16810, GQW07_13245, GRC73_17925, GRO95_10125, GRW56_14780, GRW57_16105, GUC01_17285, H0O72_17860, HEP30_002135, HEP34_002707, HHH44_001244, HI055_000900, HIE29_002967, HJQ60_000813, HLX92_13705, HLZ50_07580, HMV95_05205, HV109_19980, HV209_00945, HVV39_16975, HVW04_10850, I6H00_14750, I6H02_17970, IFB95_000680, J0541_002451, J5U05_003214, JNP96_04420, KV499_001252, NCTC10418_06269, NCTC10974_04764, NCTC11112_03242, NCTC8179_01221, NCTC9962_05868, NEP60_01835, OGM49_03465, QDW62_22280, RZR61_05910, WR15_01730, folA, tnpA
Sequence domains: Dihydrofolate reductase
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP
3 bound ligands:
Ligand MTX 1 x MTX
Ligand ACT 2 x ACT
Ligand CA 2 x CA
1 modified residue:
Ligand XCN 1 x XCN

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P212121
Unit cell:
a: 34.132Å b: 42.65Å c: 98.586Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.191 0.251
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Electric Fields and Enzyme Catalysis.
Fried et al. (2017)
7 more

2 mentions without citation

Probing the electrostatics of active site microenvironments along the catalytic cycle for Escherichia coli dihydrofolate reductase.
Liu et al. (2014)
1 more