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6o0o

crystal structure of BCL-2 G101V mutation with S55746

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

Apoptosis regulator Bcl-2,Bcl-2-like protein 1,Apoptosis regulator Bcl-2

Homo sapiens

UniProt P10415

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Monomer Protein 1 ;~{N}-(4-hydroxyphenyl)-3-[6-[[(3~{S})-3-(morpholin-4-ylmethyl)-3,4-dihydro-1~{H}-isoquinolin-2-yl]carbonyl]-1,3-benzodioxol-5-yl]-~{N}-phenyl-5,6,7,8-tetrahydroindolizine-1-carboxamide ; × 1 water × 1 Consistent with protein count
2 Insufficient information Monomer Protein 1 ;~{N}-(4-hydroxyphenyl)-3-[6-[[(3~{S})-3-(morpholin-4-ylmethyl)-3,4-dihydro-1~{H}-isoquinolin-2-yl]carbonyl]-1,3-benzodioxol-5-yl]-~{N}-phenyl-5,6,7,8-tetrahydroindolizine-1-carboxamide ; × 1 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

Monomer
1ysw 2o2f 2w3l 2w3l 4lvt 4lvt 4lxd 4man 4man 6gl8 7lhb 7lhb

13 assemblies; showing the first 12

Homodimer

None

Homotetramer

None

Other homooligomers

None

Heteromeric or nucleic-acid complex
1g5m 1gjh 2o21 2o22 2xa0 2xa0 4aq3 4aq3 4aq3 4aq3 4aq3 4aq3

67 assemblies; showing the first 12

View Construct and Data Evidence
UniProt name BCL2_HUMAN
Isoform P10415-2
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–34； UniProt 1–34 Author chain A； PDBConstruct 51–166； UniProt 92–207 Author chain C； PDBConstruct 1–34； UniProt 1–34 Author chain C； PDBConstruct 51–166； UniProt 92–207

Apoptosis regulator Bcl-2,Bcl-2-like protein 1,Apoptosis regulator Bcl-2

Homo sapiens

UniProt Q07817

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Monomer Protein 1 ;~{N}-(4-hydroxyphenyl)-3-[6-[[(3~{S})-3-(morpholin-4-ylmethyl)-3,4-dihydro-1~{H}-isoquinolin-2-yl]carbonyl]-1,3-benzodioxol-5-yl]-~{N}-phenyl-5,6,7,8-tetrahydroindolizine-1-carboxamide ; × 1 water × 1 Consistent with protein count
2 Insufficient information Monomer Protein 1 ;~{N}-(4-hydroxyphenyl)-3-[6-[[(3~{S})-3-(morpholin-4-ylmethyl)-3,4-dihydro-1~{H}-isoquinolin-2-yl]carbonyl]-1,3-benzodioxol-5-yl]-~{N}-phenyl-5,6,7,8-tetrahydroindolizine-1-carboxamide ; × 1 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

Monomer
1lxl 1maz 1r2d 1r2e 1r2g 1r2h 1r2i 1ysg 1ysi 1ysn 2lpc 2m03

41 assemblies; showing the first 12

Homodimer
2b48 3inq 3wiz 3zlr 4c52 4cin 4cin 4qvx 4tuh 4tuh 4tuh 4tuh

33 assemblies; showing the first 12

Homotetramer
4c5d

1 assemblies

Other homooligomers
4ppi

1 assemblies

Heteromeric or nucleic-acid complex
1bxl 1g5j 1g5m 1gjh 2lp8 2m04 2mej 2o21 2o22 2p1l 2p1l 2p1l

120 assemblies; showing the first 12

View Construct and Data Evidence
UniProt name B2CL1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 35–50； UniProt 29–44 Author chain C； PDBConstruct 35–50； UniProt 29–44

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_id6o0o
Deposition date deposition_date2019-02-17
Structure title titlecrystal structure of BCL-2 G101V mutation with S55746
Keywords keywordsBCL-2, S55746, complex, Protein-protein interface inhibitor, resistance mutation, APOPTOSIS; APOPTOSIS
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.

6o0o__assembly_1__model_1

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

Download this curve (.dat)

6o0o__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.

6o0o__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）16.17 Å
Rg (electron density)14.52 Å
Total Rg15.75 Å
Atom count1201
Residues137
Excluded volume21191 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 6o0o__assembly_1__model_1 monomeric （1） Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 6o0o__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 (3)

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd6o0oa_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.1 — Toxins' membrane translocation domains
Superfamily Superfamily superfamilyf.1.4 — Bcl-2 inhibitors of programmed cell death
Family Family familyf.1.4.1 — Bcl-2 inhibitors of programmed cell death
Domain ID domain_idd6o0oc_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.1 — Toxins' membrane translocation domains
Superfamily Superfamily superfamilyf.1.4 — Bcl-2 inhibitors of programmed cell death
Family Family familyf.1.4.1 — Bcl-2 inhibitors of programmed cell death
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7. Citations (1)