5cbs

Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the antagonist (R)-2-amino-3-(3'-hydroxybiphenyl-3-yl)propanoic acid at 1.8A resolution

Method: X-RAY DIFFRACTION Dmax: 112.9 Å Quality: REASONABLE

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

Glutamate receptor 2,Glutamate receptor 2

Rattus norvegicus

UniProt P19491

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 413–527 Chain A; UniProt 653–797 Chain C; UniProt 413–527 Chain C; UniProt 653–797 Fragment:UNP residues 413-527,UNP residues 653-797 E42 (R)-2-amino-3-(3'-hydroxybiphenyl-3-yl)propanoic acid × 2 SO4 SULFATE ION × 5 EDO 1,2-ETHANEDIOL × 4 GOL GLYCEROL × 3 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;280 K;PEG2000, lithium sulfate and phosphate-citrate buffer pH 4.5 Resolution 1.80 Å R-free 0.219
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 413–527 Chain B; UniProt 653–797 Chain D; UniProt 413–527 Chain D; UniProt 653–797 Fragment:UNP residues 413-527,UNP residues 653-797 E42 (R)-2-amino-3-(3'-hydroxybiphenyl-3-yl)propanoic acid × 2 SO4 SULFATE ION × 5 EDO 1,2-ETHANEDIOL × 10 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;280 K;PEG2000, lithium sulfate and phosphate-citrate buffer pH 4.5 Resolution 1.80 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.

333 other PDB entries and 481 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIA2_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–117; UniProt 413–527 Author chain A; PDBConstruct 120–264; UniProt 653–797 Author chain B; PDBConstruct 3–117; UniProt 413–527 Author chain B; PDBConstruct 120–264; UniProt 653–797 Author chain C; PDBConstruct 3–117; UniProt 413–527 Author chain C; PDBConstruct 120–264; UniProt 653–797 Author chain D; PDBConstruct 3–117; UniProt 413–527 Author chain D; PDBConstruct 120–264; UniProt 653–797

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 5cbs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5cbs
Deposition date deposition_date2015-07-01
Structure title titleCrystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the antagonist (R)-2-amino-3-(3'-hydroxybiphenyl-3-yl)propanoic acid at 1.8A resolution
Keywords keywordsAMPA receptor ligand-binding domain, GluA2-S1S2J, antagonist, membrane protein, signaling protein; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.00
Radius of gyration Rg (electron density) rg_electron34.34
Forward intensity I(0) i0214594000.00
Molecular weight molecular_weight119030.0 kDa
Excluded volume excluded_volume149560 ų
Envelope volume envelope_volume193740 ų
Hydration-shell volume shell_volume47099 ų
Envelope diameter envelope_diameter117.2
Shell Rg shell_rg41.04
Envelope Rg envelope_rg34.03
Shape Rg shape_rg34.30
Total Rg total_rg34.92
Total atoms total_atoms8323
Residues n_residues1042
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 dmax112.9
Rg (real space) rg_real35.00
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real2.1460e+08
I(0) uncertainty (real space) i0_real_error3.1410e+06
Rg (reciprocal space) rg_reciprocal35.00
I(0) (reciprocal space) i0_reciprocal214600000.0000
Solution quality estimate total_estimate0.7062
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.1
Skewness Skewness skewness0.331
Kurtosis Kurtosis kurtosis-0.478
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha33860000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.903; Stabil: 1.000; Sysdev: 0.186; Positv: 1.000; Valcen: 0.999; Smooth: 0.910

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd5cbsa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamilyc.94.1 — Periplasmic binding protein-like II
Family Family familyc.94.1.1 — Phosphate binding protein-like
Domain ID domain_idd5cbsb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamilyc.94.1 — Periplasmic binding protein-like II
Family Family familyc.94.1.1 — Phosphate binding protein-like
Domain ID domain_idd5cbsc1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamilyc.94.1 — Periplasmic binding protein-like II
Family Family familyc.94.1.1 — Phosphate binding protein-like
Domain ID domain_idd5cbsc2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd5cbsd1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamilyc.94.1 — Periplasmic binding protein-like II
Family Family familyc.94.1.1 — Phosphate binding protein-like
Domain ID domain_idd5cbsd2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (8 domains)

Domain ID domain_id5cbsA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id5cbsA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id5cbsB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id5cbsB02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id5cbsC01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id5cbsC02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id5cbsD01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id5cbsD02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II

8. Citations (1)

9. Files and Curves (10)