2vyn

Structure of E.Coli GAPDH Rat Sperm GAPDH heterotetramer

Method: X-RAY DIFFRACTION Dmax: 90.7 Å Quality: GOOD

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

GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE

OrganismNot specified

UniProt P0A9B2

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–331 Chain B; UniProt 1–331 Chain C; UniProt 1–331 Non-standard monomer:Yes (specific site not provided by mmCIF) GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE × 1 (Q9ESV6) FMT FORMIC ACID × 14 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;0.2M NA FORMATE, 20% PEG 3350, 0.1M HEPES PH 7.5 Resolution 2.20 Å R-free 0.224

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.

13 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G3P1_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–331; UniProt 1–331 Author chain B; PDBConstruct 1–331; UniProt 1–331 Author chain C; PDBConstruct 1–331; UniProt 1–331

GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE

OrganismNot specified

UniProt Q9ESV6

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 102–432 Fragment:RESIDUES 102-432 Non-standard monomer:Yes (specific site not provided by mmCIF) GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE × 3 (P0A9B2) FMT FORMIC ACID × 14 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;0.2M NA FORMATE, 20% PEG 3350, 0.1M HEPES PH 7.5 Resolution 2.20 Å R-free 0.224

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9ESV6_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 4–334; UniProt 102–432

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 2vyn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2vyn
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2vyn
Deposition date deposition_date2008-07-25
Structure title titleStructure of E.Coli GAPDH Rat Sperm GAPDH heterotetramer
Keywords keywordsOXIDOREDUCTASE, GAPDH, CONTRACEPTIVE, RAT SPERM, GLYCERALDEHYDE-3-PHOSPHATE, ALPHA CHLOROHYDRIN; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.14
Radius of gyration Rg (electron density) rg_electron31.39
Forward intensity I(0) i0341774000.00
Molecular weight molecular_weight146020.0 kDa
Excluded volume excluded_volume181820 ų
Envelope volume envelope_volume214010 ų
Hydration-shell volume shell_volume53600 ų
Envelope diameter envelope_diameter98.5
Shell Rg shell_rg40.73
Envelope Rg envelope_rg31.41
Shape Rg shape_rg31.39
Total Rg total_rg32.10
Total atoms total_atoms10244
Residues n_residues1316
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 dmax90.7
Rg (real space) rg_real31.86
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real3.4180e+08
I(0) uncertainty (real space) i0_real_error4.8350e+06
Rg (reciprocal space) rg_reciprocal31.98
I(0) (reciprocal space) i0_reciprocal341800000.0000
Solution quality estimate total_estimate0.8974
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.6
Skewness Skewness skewness0.054
Kurtosis Kurtosis kurtosis-0.558
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha244300000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.978; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.758

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd2vyna1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamilyc.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family familyc.2.1.3 — Glyceraldehyde-3-phosphate dehydrogenase-like, N-terminal domain
Domain ID domain_idd2vyna2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.81 — FwdE/GAPDH domain-like
Superfamily Superfamily superfamilyd.81.1 — Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
Family Family familyd.81.1.1 — GAPDH-like
Domain ID domain_idd2vynb1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamilyc.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family familyc.2.1.3 — Glyceraldehyde-3-phosphate dehydrogenase-like, N-terminal domain
Domain ID domain_idd2vynb2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.81 — FwdE/GAPDH domain-like
Superfamily Superfamily superfamilyd.81.1 — Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
Family Family familyd.81.1.1 — GAPDH-like
Domain ID domain_idd2vync1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamilyc.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family familyc.2.1.3 — Glyceraldehyde-3-phosphate dehydrogenase-like, N-terminal domain
Domain ID domain_idd2vync2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.81 — FwdE/GAPDH domain-like
Superfamily Superfamily superfamilyd.81.1 — Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
Family Family familyd.81.1.1 — GAPDH-like

CATH v4.4 (8 domains)

Domain ID domain_id2vynA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily720 — NAD(P)-binding Rossmann-like Domain
Domain ID domain_id2vynA02
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_id2vynB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily720 — NAD(P)-binding Rossmann-like Domain
Domain ID domain_id2vynB02
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_id2vynC01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily720 — NAD(P)-binding Rossmann-like Domain
Domain ID domain_id2vynC02
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_id2vynD01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily720 — NAD(P)-binding Rossmann-like Domain
Domain ID domain_id2vynD02
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)