3v3k

Human caspase 9 in complex with bacterial effector protein

Method: X-RAY DIFFRACTION

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

Caspase-9

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Putative uncharacterized protein ECs1815 × 1 （Q8XAL7）	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Putative uncharacterized protein ECs1815 × 1 （Q8XAL7）	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	Putative uncharacterized protein ECs1815 × 1 （Q8XAL7）	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 2	Putative uncharacterized protein ECs1815 × 1 （Q8XAL7）	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 2	Putative uncharacterized protein ECs1815 × 1 （Q8XAL7）	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 2	Putative uncharacterized protein ECs1815 × 1 （Q8XAL7）	Consistent with protein count
7	Protein heterocomplex	Heteromer	Protein 2	Putative uncharacterized protein ECs1815 × 1 （Q8XAL7）	Consistent with protein count
8	Protein heterocomplex	Heteromer	Protein 2	Putative uncharacterized protein ECs1815 × 1 （Q8XAL7）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CASP9_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–276； UniProt 141–416 Author chain C； PDBConstruct 1–276； UniProt 141–416 Author chain E； PDBConstruct 1–276； UniProt 141–416 Author chain G； PDBConstruct 1–276； UniProt 141–416 Author chain I； PDBConstruct 1–276； UniProt 141–416 Author chain K； PDBConstruct 1–276； UniProt 141–416 Author chain M； PDBConstruct 1–276； UniProt 141–416 Author chain O； PDBConstruct 1–276； UniProt 141–416

Putative uncharacterized protein ECs1815

Escherichia coli O157:H7

UniProt Q8XAL7

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Caspase-9 × 1 （P55211）	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Caspase-9 × 1 （P55211）	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	Caspase-9 × 1 （P55211）	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 2	Caspase-9 × 1 （P55211）	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 2	Caspase-9 × 1 （P55211）	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 2	Caspase-9 × 1 （P55211）	Consistent with protein count
7	Protein heterocomplex	Heteromer	Protein 2	Caspase-9 × 1 （P55211）	Consistent with protein count
8	Protein heterocomplex	Heteromer	Protein 2	Caspase-9 × 1 （P55211）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q8XAL7_ECO57
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–165； UniProt 25–189 Author chain D； PDBConstruct 1–165； UniProt 25–189 Author chain F； PDBConstruct 1–165； UniProt 25–189 Author chain H； PDBConstruct 1–165； UniProt 25–189 Author chain J； PDBConstruct 1–165； UniProt 25–189 Author chain L； PDBConstruct 1–165； UniProt 25–189 Author chain N； PDBConstruct 1–165； UniProt 25–189 Author chain P； PDBConstruct 1–165； UniProt 25–189

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_id	3v3k
Deposition date deposition_date	2011-12-13
Structure title title	Human caspase 9 in complex with bacterial effector protein
Keywords keywords	HYDROLASE, Caspase 9; HYDROLASE
Experimental Method method	X-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.

3v3k__assembly_1__model_1

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

Download this curve (.dat)

3v3k__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3v3k__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	24.96 Å
Rg (electron density)	24.21 Å
Total Rg	25.06 Å
Atom count	3217
Residues	410
Excluded volume	57116 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3v3k__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3v3k__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`3v3k__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`3v3k__assembly_4__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`3v3k__assembly_5__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
6	1	`3v3k__assembly_6__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
7	1	`3v3k__assembly_7__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
8	1	`3v3k__assembly_8__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 (2)

Entity 1 Entity 1 polymer

Description description	Caspase-9
Molecular weight formula_weight	30416.6 kDa
EC 编号 ec_number	3.4.22.62
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,E,G,I,K,M,O
Atom count atom_count	25428

ALESLRGNADLAYILSMEPCGHCLIINNVNFCRESGLRTRTGSNIDCEKLRRRFSSLHFMVEVKGDLTAKKMVLALLELARQDHGALDCCVVVILSHGCQASHLQFPGAVYGTDGCPVSVEKIVNIFNGTSCPSLGGKPKLFFIQACGGEQKDHGFEVASTSPEDESPGSNPEPDATPFQEGLRTFDQLDAISSLPTPSDIFVSYSTFPGFVSWRDPKSGSWYVETLDDIFEQWAHSEDLQSLLLRVANAVSVKGIYKQMPGCFNFLRKKLFFKTS

Source Source

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Putative uncharacterized protein ECs1815
Molecular weight formula_weight	18866.2 kDa
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D,F,H,J,L,N,P

TPESVSELNHNHFLSPELQDKLDVMVSIYSCARNNNELEEIFQELSAFVSGLMDKRNSVFEVRNENTDEVVGALRAGMTIEDRDSYIRDLFFLHSLKVKIEESRQGKEDSKCKVYNLLCPHHSSELYGDLRAMKCLVEGCSDDFNPFDIIRVPDLTYNKGSLQCG

Source Source

Source organism organism	Escherichia coli O157:H7
NCBI taxonomy ID ncbi_taxonomy_id	83334
Host organism host_organism	Escherichia coli

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6. Fold Classification (SCOP + CATH) 16 domains

CATH v4.4 (16 domains)

Domain ID domain_id	3v3kA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1460 —

Domain ID domain_id	3v3kB00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1260 — Ferritin
Homologous superfamily homologous superfamily	90 —

Domain ID domain_id	3v3kC00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1460 —

Domain ID domain_id	3v3kD00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1260 — Ferritin
Homologous superfamily homologous superfamily	90 —

Domain ID domain_id	3v3kE00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1460 —

Domain ID domain_id	3v3kF00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1260 — Ferritin
Homologous superfamily homologous superfamily	90 —

Domain ID domain_id	3v3kG00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1460 —

Domain ID domain_id	3v3kH00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1260 — Ferritin
Homologous superfamily homologous superfamily	90 —

Domain ID domain_id	3v3kI00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1460 —

Domain ID domain_id	3v3kJ00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1260 — Ferritin
Homologous superfamily homologous superfamily	90 —

Domain ID domain_id	3v3kK00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1460 —

Domain ID domain_id	3v3kL00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1260 — Ferritin
Homologous superfamily homologous superfamily	90 —

Domain ID domain_id	3v3kM00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1460 —

Domain ID domain_id	3v3kN00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1260 — Ferritin
Homologous superfamily homologous superfamily	90 —

Domain ID domain_id	3v3kO00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1460 —

Domain ID domain_id	3v3kP00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1260 — Ferritin
Homologous superfamily homologous superfamily	90 —

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Unit-cell length a length_a	100.703 Å
Unit-cell length b length_b	209.906 Å
Unit-cell length c length_c	317.231 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	32

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	3.494 Å
Low-resolution limit resolution_low	174.080 Å
R factor r_factor	0.2396
R_work r_work	0.2392
R_free r_free	0.2595

Human caspase 9 in complex with bacterial effector protein

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

Caspase-9

State in the Current Structure

Other States of the Same Protein in the Database

Putative uncharacterized protein ECs1815

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

3v3k__assembly_1__model_1

3v3k__assembly_1__model_1 | I(q)

3v3k__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 16 domains

CATH v4.4 (16 domains)

7. Citations (1)

Human caspase 9 in complex with bacterial effector protein

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

Caspase-9

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Putative uncharacterized protein ECs1815

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

3v3k__assembly_1__model_1

3v3k__assembly_1__model_1 | I(q)

3v3k__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 16 domains

CATH v4.4 (16 domains)

7. Citations (1)