2qd2

F110A variant of human ferrochelatase with protoheme bound

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

Ferrochelatase

Homo sapiens

UniProt Q7KZA3

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 BICARBONATE ION × 2 FE2/S2 (INORGANIC) CLUSTER × 2 IMIDAZOLE × 3 CHOLIC ACID × 4 PROTOPORPHYRIN IX CONTAINING FE × 2 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name Q7KZA3_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–359; UniProt 58–416 Author chain B; PDBConstruct 1–359; UniProt 58–416

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_id2qd2
Deposition date deposition_date2007-06-20
Structure title titleF110A variant of human ferrochelatase with protoheme bound
Keywords keywordsHeme synthesis, Ferrochelatase, Protoporphyrin IX, Heme biosynthesis, Iron, Lyase, Porphyrin biosynthesis, BIOSYNTHETIC PROTEIN; BIOSYNTHETIC PROTEIN
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.

2qd2__assembly_1__model_1

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

Download this curve (.dat)

2qd2__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.

2qd2__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)27.72 Å
Rg (electron density)26.71 Å
Total Rg27.54 Å
Atom count6003
Residues718
Excluded volume107910 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2qd2__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 (7)

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2qd2a_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.92 — Chelatase-like
Superfamily Superfamily superfamilyc.92.1 — Chelatase
Family Family familyc.92.1.1 — Ferrochelatase
Domain ID domain_idd2qd2b_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.92 — Chelatase-like
Superfamily Superfamily superfamilyc.92.1 — Chelatase
Family Family familyc.92.1.1 — Ferrochelatase

CATH v4.4 (4 domains)

Domain ID domain_id2qd2A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1400 —
Domain ID domain_id2qd2A02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1400 —
Domain ID domain_id2qd2B01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1400 —
Domain ID domain_id2qd2B02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1400 —
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7. Citations (1)