5vfj

Crystal structure of BnSP-7 from bothrops pauloensis complexed with caffeic acid

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

Basic phospholipase A2 homolog BnSP-7

OrganismNot specified

UniProt Q9IAT9

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 SULFATE ION × 5 CAFFEIC ACID × 1 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name PA2H_BOTPA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–121; UniProt 1–120 Author chain B; PDBConstruct 2–121; UniProt 1–120

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_id5vfj
Deposition date deposition_date2017-04-07
Structure title titleCrystal structure of BnSP-7 from bothrops pauloensis complexed with caffeic acid
Keywords keywordsLys49-PLA2, Bothrops pauloensis, Caffeic acid, 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.

5vfj__assembly_1__model_1

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

Download this curve (.dat)

5vfj__assembly_1__model_1 | I(q)

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

5vfj__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)20.03 Å
Rg (electron density)19.26 Å
Total Rg20.07 Å
Atom count1908
Residues242
Excluded volume33768 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 5vfj__assembly_1__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) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd5vfja1
Class classa — All alpha proteins
Fold Fold folda.133 — Phospholipase A2, PLA2
Superfamily Superfamily superfamilya.133.1 — Phospholipase A2, PLA2
Family Family familya.133.1.2 — Vertebrate phospholipase A2
Domain ID domain_idd5vfja2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd5vfjb1
Class classa — All alpha proteins
Fold Fold folda.133 — Phospholipase A2, PLA2
Superfamily Superfamily superfamilya.133.1 — Phospholipase A2, PLA2
Family Family familya.133.1.2 — Vertebrate phospholipase A2
Domain ID domain_idd5vfjb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id5vfjA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology90 — Phospholipase A2
Homologous superfamily homologous superfamily10 — Phospholipase A2 domain
Domain ID domain_id5vfjB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology90 — Phospholipase A2
Homologous superfamily homologous superfamily10 — Phospholipase A2 domain
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7. Citations (1)