3ba0

Crystal structure of full-length human MMP-12

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

Macrophage metalloelastase

Homo sapiens

UniProt P39900

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 × 4 ACETOHYDROXAMIC ACID × 1 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name MMP12_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–365; UniProt 106–470

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_id3ba0
Deposition date deposition_date2007-11-07
Structure title titleCrystal structure of full-length human MMP-12
Keywords keywords;Full-length MMP-12, hemopexin domain, catalytic domain, domain interaction., Calcium, Extracellular matrix, Glycoprotein, Hydrolase, Metal-binding, Metalloprotease, Polymorphism, Protease, Secreted, Zinc, Zymogen ;; 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.

3ba0__assembly_1__model_1

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

Download this curve (.dat)

3ba0__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.

3ba0__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)27.93 Å
Rg (electron density)27.38 Å
Total Rg28.10 Å
Atom count3001
Residues365
Excluded volume53315 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 3ba0__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 (5)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3ba0a1
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.92.1.11 — Matrix metalloproteases, catalytic domain
Domain ID domain_idd3ba0a2
Class classb — All beta proteins
Fold Fold foldb.66 — 4-bladed beta-propeller
Superfamily Superfamily superfamilyb.66.1 — Hemopexin-like domain
Family Family familyb.66.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id3ba0A01
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_id3ba0A02
Class class2 — Mainly Beta
Architecture architecture110 — 4 Propeller
Topology topology10 — Hemopexin
Homologous superfamily homologous superfamily10 — Hemopexin-like domain
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7. Citations (3)