5zmw

Crystal structure of the E309Q mutant of SR Ca2+-ATPase in E2(TG)

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

Sarcoplasmic/endoplasmic reticulum calcium ATPase 1

Oryctolagus cuniculus

UniProt P04191

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 SODIUM ION × 1 SULFATE ION × 1 ;OCTANOIC ACID [3S-[3ALPHA, 3ABETA, 4ALPHA, 6BETA, 6ABETA, 7BETA, 8ALPHA(Z), 9BALPHA]]-6-(ACETYLOXY)-2,3,-3A,4,5,6,6A,7,8,9B-DECAHYDRO-3,3A-DIHYDROXY-3,6,9-TRIMETHYL-8-[(2-METHYL-1-OXO-2-BUTENYL)OX Y]-2-OXO-4-(1-OXOBUTOXY)-AZULENO[4,5-B]FURAN-7-YL ESTER ; × 1 DECYL-BETA-D-MALTOPYRANOSIDE × 2 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name AT2A1_RABIT
Isoform P04191-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–1000; UniProt 1–994

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_id5zmw
Deposition date deposition_date2018-04-06
Structure title titleCrystal structure of the E309Q mutant of SR Ca2+-ATPase in E2(TG)
Keywords keywords;MEMBRANE PROTEIN, P-TYPE ATPASE, HAD FOLD, ATP-BINDING, CALCIUM TRANSPORT, ENDOPLASMIC RETICULUM, ION TRANSPORT, MAGNESIUM, METAL-BINDING, NUCLEOTIDE-BINDING, PHOSPHORYLATION, SARCOPLASMIC RETICULUM, TRANSMEMBRANE, TRANSPORT, HYDROLASE ;; HYDROLASE
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.

5zmw__assembly_1__model_1

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

Download this curve (.dat)

5zmw__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

5zmw__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)38.12 Å
Rg (electron density)38.59 Å
Total Rg38.59 Å
Atom count7829
Residues1000
Excluded volume140920 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 5zmw__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 (6)

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6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id5zmwA01
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology150 — Calcium-transporting ATPase, cytoplasmic transduction domain A
Homologous superfamily homologous superfamily10 — Calcium-transporting ATPase, cytoplasmic transduction domain A
Domain ID domain_id5zmwA02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1110 — Calcium-transporting ATPase, transmembrane domain
Homologous superfamily homologous superfamily10 — Calcium-transporting ATPase, transmembrane domain
Domain ID domain_id5zmwA03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1000 — HAD superfamily/HAD-like
Domain ID domain_id5zmwA04
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1110 — Calcium-transporting ATPase, cytoplasmic domain N
Homologous superfamily homologous superfamily10 — Calcium-transporting ATPase, cytoplasmic domain N
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7. Citations (1)