4r3v

Structure of karilysin propeptide and catalytic MMP domain

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

Karilysin

Tannerella forsythia

UniProt D0EM77

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 CALCIUM ION × 1 GLYCEROL × 3 water × 1 Consistent with protein count
2 Protein monomer Monomer Protein 1 ZINC ION × 2 CALCIUM ION × 1 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name KLY_TANFA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–183; UniProt 21–201 Author chain B; PDBConstruct 3–183; UniProt 21–201

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_id4r3v
Deposition date deposition_date2014-08-18
Structure title titleStructure of karilysin propeptide and catalytic MMP domain
Keywords keywords;Metzincin metallopeptidase, Matrix metalloproteinase with unique propeptide, Bacterial matrix metalloproteinase-like enzyme, 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.

4r3v__assembly_1__model_1

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

Download this curve (.dat)

4r3v__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.

4r3v__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)16.39 Å
Rg (electron density)15.08 Å
Total Rg16.22 Å
Atom count1438
Residues179
Excluded volume25275 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 4r3v__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 4r3v__assembly_2__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 (5)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4r3va_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.92 — Zincin-like
Superfamily Superfamily superfamilyd.92.1 — Metalloproteases ('zincins'), catalytic domain
Family Family familyd.92.1.0 — automated matches
Domain ID domain_idd4r3vb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.92 — Zincin-like
Superfamily Superfamily superfamilyd.92.1 — Metalloproteases ('zincins'), catalytic domain
Family Family familyd.92.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id4r3vA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology390 — Collagenase (Catalytic Domain)
Homologous superfamily homologous superfamily10 — Collagenase (Catalytic Domain)
Domain ID domain_id4r3vB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology390 — Collagenase (Catalytic Domain)
Homologous superfamily homologous superfamily10 — Collagenase (Catalytic Domain)
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7. Citations (1)