5vmt

Crystal structure of a glyceraldehyde-3-phosphate dehydrogenase from Neisseria gonorrhoeae bound to NAD

Method: X-RAY DIFFRACTION Dmax: 163.8 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Glyceraldehyde-3-phosphate dehydrogenase

Neisseria gonorrhoeae

UniProt B4RPP8

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 24–357 Chain B; UniProt 24–357 Chain C; UniProt 24–357 Chain D; UniProt 24–357 Fragment:residues 24-357 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 CL CHLORIDE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;289 K;NegoA.00617.a.B1.PS38018 at 21.2 mg/mL with 3 mM NAD against JCSG+ screen condition A9 0.2 M ammonium chloride, 25% PEG 3350 supplemented with 20% ethylene glycol and 3 mM NAD as cryoprotectant, crystal tracking ID 284230a9, unique puck ID giy4-10 Resolution 2.50 Å R-free 0.219
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 24–357 Chain F; UniProt 24–357 Chain G; UniProt 24–357 Chain H; UniProt 24–357 Fragment:residues 24-357 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;289 K;NegoA.00617.a.B1.PS38018 at 21.2 mg/mL with 3 mM NAD against JCSG+ screen condition A9 0.2 M ammonium chloride, 25% PEG 3350 supplemented with 20% ethylene glycol and 3 mM NAD as cryoprotectant, crystal tracking ID 284230a9, unique puck ID giy4-10 Resolution 2.50 Å R-free 0.219

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

4 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B4RPP8_NEIG2
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 9–342; UniProt 24–357 Author chain B; PDBConstruct 9–342; UniProt 24–357 Author chain C; PDBConstruct 9–342; UniProt 24–357 Author chain D; PDBConstruct 9–342; UniProt 24–357 Author chain E; PDBConstruct 9–342; UniProt 24–357 Author chain F; PDBConstruct 9–342; UniProt 24–357 Author chain G; PDBConstruct 9–342; UniProt 24–357 Author chain H; PDBConstruct 9–342; UniProt 24–357

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 5vmt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5vmt
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5vmt
Deposition date deposition_date2017-04-28
Structure title titleCrystal structure of a glyceraldehyde-3-phosphate dehydrogenase from Neisseria gonorrhoeae bound to NAD
Keywords keywords;NIAID, structural genomics, co-factor, glycolysis, Seattle Structural Genomics Center for Infectious Disease, SSGCID, OXIDOREDUCTASE ;; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier47.77
Radius of gyration Rg (electron density) rg_electron47.86
Forward intensity I(0) i01174200000.00
Molecular weight molecular_weight275920.0 kDa
Excluded volume excluded_volume341480 ų
Envelope volume envelope_volume445410 ų
Hydration-shell volume shell_volume76634 ų
Envelope diameter envelope_diameter166.1
Shell Rg shell_rg52.63
Envelope Rg envelope_rg47.09
Shape Rg shape_rg47.89
Total Rg total_rg47.91
Total atoms total_atoms19374
Residues n_residues2616
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax163.8
Rg (real space) rg_real47.97
Rg uncertainty (real space) rg_real_error1.54
I(0) (real space) i0_real1.1740e+09
I(0) uncertainty (real space) i0_real_error1.9170e+07
Rg (reciprocal space) rg_reciprocal47.78
I(0) (reciprocal space) i0_reciprocal1174000000.0000
Solution quality estimate total_estimate0.8623
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.6
Skewness Skewness skewness0.398
Kurtosis Kurtosis kurtosis-0.490
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha107400000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.808; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.799

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id5vmtA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology360 — Dihydrodipicolinate Reductase; domain 2
Homologous superfamily homologous superfamily10 — Dihydrodipicolinate Reductase; domain 2
Domain ID domain_id5vmtB02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology360 — Dihydrodipicolinate Reductase; domain 2
Homologous superfamily homologous superfamily10 — Dihydrodipicolinate Reductase; domain 2
Domain ID domain_id5vmtC02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology360 — Dihydrodipicolinate Reductase; domain 2
Homologous superfamily homologous superfamily10 — Dihydrodipicolinate Reductase; domain 2
Domain ID domain_id5vmtD02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology360 — Dihydrodipicolinate Reductase; domain 2
Homologous superfamily homologous superfamily10 — Dihydrodipicolinate Reductase; domain 2
Domain ID domain_id5vmtE02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology360 — Dihydrodipicolinate Reductase; domain 2
Homologous superfamily homologous superfamily10 — Dihydrodipicolinate Reductase; domain 2
Domain ID domain_id5vmtF02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology360 — Dihydrodipicolinate Reductase; domain 2
Homologous superfamily homologous superfamily10 — Dihydrodipicolinate Reductase; domain 2
Domain ID domain_id5vmtG02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology360 — Dihydrodipicolinate Reductase; domain 2
Homologous superfamily homologous superfamily10 — Dihydrodipicolinate Reductase; domain 2
Domain ID domain_id5vmtH02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology360 — Dihydrodipicolinate Reductase; domain 2
Homologous superfamily homologous superfamily10 — Dihydrodipicolinate Reductase; domain 2

8. Citations (1)

9. Files and Curves (10)