1mh6

Solution Structure of the Transposon Tn5-encoding Bleomycin-binding Protein, BLMT

Method: SOLUTION NMR

1. Protein Identity and Related Structures Protein Identity & Related Structures

BLEOMYCIN RESISTANCE PROTEIN

Klebsiella pneumoniae

UniProt P13081

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name BLE_KLEPN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–125; UniProt 2–126 Author chain B; PDBConstruct 1–125; UniProt 2–126

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.

2. Structure Basics 2. Structure Basics

Entry ID entry_id1mh6
Deposition date deposition_date2002-08-19
Structure title titleSolution Structure of the Transposon Tn5-encoding Bleomycin-binding Protein, BLMT
Keywords keywordsAntibiotic resistance, Transposable element, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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.

1mh6__assembly_1__model_1

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

Download this curve (.dat)

1mh6__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.

1mh6__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)18.96 Å
Rg (electron density)17.82 Å
Total Rg18.77 Å
Atom count3838
Residues250
Excluded volume34583 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1mh6__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download

4. Crystallography and Experiment 4. Crystallography & Experiment

5. Entities and Polymers Entities & Polymers (1)

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1mh6a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.32 — Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Superfamily Superfamily superfamilyd.32.1 — Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Family Family familyd.32.1.2 — Antibiotic resistance proteins
Domain ID domain_idd1mh6b_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.32 — Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Superfamily Superfamily superfamilyd.32.1 — Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Family Family familyd.32.1.2 — Antibiotic resistance proteins

CATH v4.4 (2 domains)

Domain ID domain_id1mh6A00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology180 — 2,3-Dihydroxybiphenyl 1,2-Dioxygenase; domain 1
Homologous superfamily homologous superfamily10 — 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1
Domain ID domain_id1mh6B00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology180 — 2,3-Dihydroxybiphenyl 1,2-Dioxygenase; domain 1
Homologous superfamily homologous superfamily10 — 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1

7. Citations (1)