2mjw

Structural Insights into Calcium Bound S100P - V Domain of the receptor for advanced glycation end products (RAGE) Complex

Method: SOLUTION NMR
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Advanced glycosylation end product-specific receptor

Homo sapiens

UniProt Q15109

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 Protein S100-P × 2 (P25815) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name RAGE_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–101; UniProt 23–121 Author chain C; PDBConstruct 3–101; UniProt 23–121

Protein S100-P

Homo sapiens

UniProt P25815

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 Advanced glycosylation end product-specific receptor × 2 (Q15109) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name S100P_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–94; UniProt 1–94 Author chain D; PDBConstruct 1–94; UniProt 1–94

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_id2mjw
Deposition date deposition_date2014-01-19
Structure title titleStructural Insights into Calcium Bound S100P - V Domain of the receptor for advanced glycation end products (RAGE) Complex
Keywords keywordsS100P V Domain of RAGE, SIGNALING PROTEIN-METAL BINDING PROTEIN complex; SIGNALING PROTEIN/METAL BINDING PROTEIN
Experimental Method methodSOLUTION NMR
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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.

2mjw__assembly_1__model_8

Assembly 1 · Model 8 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2mjw__assembly_1__model_8 | I(q)

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

2mjw__assembly_1__model_8 | 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)24.20 Å
Rg (electron density)23.26 Å
Total Rg24.24 Å
Atom count6072
Residues390
Excluded volume53998 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2mjw__assembly_1__model_1 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 2mjw__assembly_1__model_2 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 2mjw__assembly_1__model_3 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 2mjw__assembly_1__model_4 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 2mjw__assembly_1__model_5 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
1 6 2mjw__assembly_1__model_6 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
1 7 2mjw__assembly_1__model_7 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
1 8 2mjw__assembly_1__model_8 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
1 9 2mjw__assembly_1__model_9 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
1 10 2mjw__assembly_1__model_10 tetrameric (4) 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 (2)

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2mjwb_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.2 — S100 proteins
Domain ID domain_idd2mjwd_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.2 — S100 proteins

CATH v4.4 (4 domains)

Domain ID domain_id2mjwA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2mjwB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id2mjwC00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2mjwD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
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7. Citations (1)