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2i3v

Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of G725C mutant

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Glutamate receptor 2

Rattus norvegicus

UniProt P19491

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 ZINC ION × 2 GLUTAMIC ACID × 1 water × 1 Consistent with protein count
2 Protein monomer Monomer Protein 1 ZINC ION × 3 GLUTAMIC ACID × 1 water × 1 Consistent with protein count
3 Protein monomer Monomer Protein 1 ZINC ION × 1 GLUTAMIC ACID × 1 water × 1 Consistent with protein count
4 Protein monomer Monomer Protein 1 ZINC ION × 1 GLUTAMIC ACID × 1 water × 1 Consistent with protein count
5 Protein homooligomer Homooligomer Protein 4 ZINC ION × 7 GLUTAMIC ACID × 4 water × 4 Consistent with protein count
6 Protein homooligomer Homooligomer Protein 2 ZINC ION × 4 GLUTAMIC ACID × 2 water × 2 Consistent with protein count
7 Protein homooligomer Homooligomer Protein 2 ZINC ION × 3 GLUTAMIC ACID × 2 water × 2 Consistent with protein count
8 Protein homooligomer Homooligomer Protein 2 ZINC ION × 4 GLUTAMIC ACID × 2 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

Monomer
1ftj 1ftj 1ftj 1ftk 1ftm 1ftm 1ftm 1fto 1fto 1fw0 1gr2 1lb8

57 assemblies; showing the first 12

Homodimer
1ftj 1ftl 1ftm 1m5b 1m5b 1m5c 1m5d 1m5e 1m5e 1m5f 1m5f 1mm6

242 assemblies; showing the first 12

Homotetramer
2i3v 4u1w 4u1x 4u1y 4u2p 4u2q 4u2r 4uq6 4uqj 4uqk 5jei 5kbv

48 assemblies; showing the first 12

Other homooligomers
1ftj 1ftm 1m5b 1m5e 1m5f 1ms7 1mxu 1mxv 1mxw 1mxx 1mxy 1mxz

21 assemblies; showing the first 12

Heteromeric or nucleic-acid complex
3h5v 3hsy 3kg2 4u4f 4u4g 4u5b 4u5c 4u5d 4u5e 4u5f 5fwx 5fwx

115 assemblies; showing the first 12

View Construct and Data Evidence
UniProt name GRIA2_RAT
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–115； UniProt 413–527 Author chain A； PDBConstruct 118–259； UniProt 653–794 Author chain B； PDBConstruct 1–115； UniProt 413–527 Author chain B； PDBConstruct 118–259； UniProt 653–794 Author chain C； PDBConstruct 1–115； UniProt 413–527 Author chain C； PDBConstruct 118–259； UniProt 653–794 Author chain D； PDBConstruct 1–115； UniProt 413–527 Author chain D； PDBConstruct 118–259； UniProt 653–794

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id2i3v
Deposition date deposition_date2006-08-21
Structure title titleMeasurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of G725C mutant
Keywords keywordsIonotropic glutamate receptor ligand binding core S1S2 G725C mutant, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

2i3v__assembly_7__model_1

Assembly 7 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2i3v__assembly_7__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

2i3v__assembly_7__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg（Guinier）26.44 Å
Rg (electron density)25.53 Å
Total Rg26.49 Å
Atom count4073
Residues517
Excluded volume73347 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2i3v__assembly_1__model_1 monomeric （1） Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 2i3v__assembly_2__model_1 monomeric （1） Success 4.1.3-1-20251215 (887e7ef) View Download
3 1 2i3v__assembly_3__model_1 monomeric （1） Success 4.1.3-1-20251215 (887e7ef) View Download
4 1 2i3v__assembly_4__model_1 monomeric （1） Success 4.1.3-1-20251215 (887e7ef) View Download
5 1 2i3v__assembly_5__model_1 tetrameric （4） Success 4.1.3-1-20251215 (887e7ef) View Download
6 1 2i3v__assembly_6__model_1 dimeric （2） Success 4.1.3-1-20251215 (887e7ef) View Download
7 1 2i3v__assembly_7__model_1 dimeric （2） Success 4.1.3-1-20251215 (887e7ef) View Download
8 1 2i3v__assembly_8__model_1 dimeric （2） Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (4)

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6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2i3va_
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_idd2i3vb_
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_idd2i3vc_
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_idd2i3vd_
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

CATH v4.4 (8 domains)

Domain ID domain_id2i3vA01
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_id2i3vA02
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_id2i3vB01
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_id2i3vB02
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_id2i3vC01
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_id2i3vC02
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_id2i3vD01
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_id2i3vD02
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
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7. Citations (2)