1mmo

CRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANE

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

METHANE MONOOXYGENASE HYDROLASE (BETA CHAIN)

Methylococcus capsulatus

UniProt P18798

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 6 METHANE MONOOXYGENASE HYDROLASE (ALPHA CHAIN) × 2 (P22869) METHANE MONOOXYGENASE HYDROLASE (GAMMA CHAIN) × 2 (P11987) FE (III) ION × 4 ACETIC ACID × 2 water × 6 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name MEMB_METCA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–384; UniProt 6–389 Author chain C; PDBConstruct 1–384; UniProt 6–389

METHANE MONOOXYGENASE HYDROLASE (ALPHA CHAIN)

Methylococcus capsulatus

UniProt P22869

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 6 METHANE MONOOXYGENASE HYDROLASE (BETA CHAIN) × 2 (P18798) METHANE MONOOXYGENASE HYDROLASE (GAMMA CHAIN) × 2 (P11987) FE (III) ION × 4 ACETIC ACID × 2 water × 6 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name MEMA_METCA
Isoform —
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–512; UniProt 15–526 Author chain E; PDBConstruct 1–512; UniProt 15–526

METHANE MONOOXYGENASE HYDROLASE (GAMMA CHAIN)

Methylococcus capsulatus

UniProt P11987

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 6 METHANE MONOOXYGENASE HYDROLASE (BETA CHAIN) × 2 (P18798) METHANE MONOOXYGENASE HYDROLASE (ALPHA CHAIN) × 2 (P22869) FE (III) ION × 4 ACETIC ACID × 2 water × 6 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name MEMG_METCA
Isoform —
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–162; UniProt 3–164 Author chain H; PDBConstruct 1–162; UniProt 3–164

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_id1mmo
Deposition date deposition_date1994-02-22
Structure title titleCRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANE
Keywords keywordsOXIDOREDUCTASE (MONOOXYGENASE); OXIDOREDUCTASE (MONOOXYGENASE)
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.

1mmo__assembly_1__model_1

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

Download this curve (.dat)

1mmo__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.

1mmo__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)41.45 Å
Rg (electron density)41.07 Å
Total Rg41.45 Å
Atom count21282
Residues2116
Excluded volume306440 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1mmo__assembly_1__model_1 hexameric (6) 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) 14 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1mmob_
Class classa — All alpha proteins
Fold Fold folda.25 — Ferritin-like
Superfamily Superfamily superfamilya.25.1 — Ferritin-like
Family Family familya.25.1.2 — Ribonucleotide reductase-like
Domain ID domain_idd1mmoc_
Class classa — All alpha proteins
Fold Fold folda.25 — Ferritin-like
Superfamily Superfamily superfamilya.25.1 — Ferritin-like
Family Family familya.25.1.2 — Ribonucleotide reductase-like
Domain ID domain_idd1mmod_
Class classa — All alpha proteins
Fold Fold folda.25 — Ferritin-like
Superfamily Superfamily superfamilya.25.1 — Ferritin-like
Family Family familya.25.1.2 — Ribonucleotide reductase-like
Domain ID domain_idd1mmoe_
Class classa — All alpha proteins
Fold Fold folda.25 — Ferritin-like
Superfamily Superfamily superfamilya.25.1 — Ferritin-like
Family Family familya.25.1.2 — Ribonucleotide reductase-like
Domain ID domain_idd1mmog_
Class classa — All alpha proteins
Fold Fold folda.23 — Open three-helical up-and-down bundle
Superfamily Superfamily superfamilya.23.3 — Methane monooxygenase hydrolase, gamma subunit
Family Family familya.23.3.1 — Methane monooxygenase hydrolase, gamma subunit
Domain ID domain_idd1mmoh_
Class classa — All alpha proteins
Fold Fold folda.23 — Open three-helical up-and-down bundle
Superfamily Superfamily superfamilya.23.3 — Methane monooxygenase hydrolase, gamma subunit
Family Family familya.23.3.1 — Methane monooxygenase hydrolase, gamma subunit

CATH v4.4 (8 domains)

Domain ID domain_id1mmoB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology620 — Ribonucleotide Reductase, subunit A
Homologous superfamily homologous superfamily20 — Ribonucleotide Reductase, subunit A
Domain ID domain_id1mmoC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology620 — Ribonucleotide Reductase, subunit A
Homologous superfamily homologous superfamily20 — Ribonucleotide Reductase, subunit A
Domain ID domain_id1mmoD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology620 — Ribonucleotide Reductase, subunit A
Homologous superfamily homologous superfamily20 — Ribonucleotide Reductase, subunit A
Domain ID domain_id1mmoE00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology620 — Ribonucleotide Reductase, subunit A
Homologous superfamily homologous superfamily20 — Ribonucleotide Reductase, subunit A
Domain ID domain_id1mmoG01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily10 — Methane monooxygenase, gamma chain, domain 1
Domain ID domain_id1mmoG02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily30 — Methane monooxygenase, gamma chain, domain 2
Domain ID domain_id1mmoH01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily10 — Methane monooxygenase, gamma chain, domain 1
Domain ID domain_id1mmoH02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily30 — Methane monooxygenase, gamma chain, domain 2
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7. Citations (1)