1m3g

SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF MAPK PHOSPHATASE PAC-1: INSIGHTS INTO SUBSTRATE-INDUCED ENZYMATIC ACTIVATION

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

DUAL SPECIFICITY PROTEIN PHOSPHATASE 2

Homo sapiens

UniProt Q05923

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name DUS2_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–145; UniProt 170–314

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_id1m3g
Deposition date deposition_date2002-06-27
Structure title titleSOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF MAPK PHOSPHATASE PAC-1: INSIGHTS INTO SUBSTRATE-INDUCED ENZYMATIC ACTIVATION
Keywords keywordsCATALYTIC DOMAIN, MAPK PHOSPHATASE, PAC-1, HYDROLASE; HYDROLASE
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.

1m3g__assembly_1__model_1

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

Download this curve (.dat)

1m3g__assembly_1__model_1 | I(q)

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

1m3g__assembly_1__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)16.20 Å
Rg (electron density)14.72 Å
Total Rg15.91 Å
Atom count2248
Residues145
Excluded volume20139 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1m3g__assembly_1__model_1 monomeric (1) 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 (1)

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1m3ga_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.45 — (Phosphotyrosine protein) phosphatases II
Superfamily Superfamily superfamilyc.45.1 — (Phosphotyrosine protein) phosphatases II
Family Family familyc.45.1.1 — Dual specificity phosphatase-like

CATH v4.4 (1 domains)

Domain ID domain_id1m3gA00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology190 — Protein-Tyrosine Phosphatase; Chain A
Homologous superfamily homologous superfamily10 — Protein tyrosine phosphatase superfamily
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7. Citations (1)