2qw7

Carboxysome Subunit, CcmL

Method: X-RAY DIFFRACTION

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

Carbon dioxide concentrating mechanism protein ccmL

Synechocystis sp.

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 5	GLYCEROL × 2 water × 5	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 5	GLYCEROL × 2 water × 5	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CCML_SYNY3
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–100； UniProt 1–100 Author chain B； PDBConstruct 1–100； UniProt 1–100 Author chain C； PDBConstruct 1–100； UniProt 1–100 Author chain D； PDBConstruct 1–100； UniProt 1–100 Author chain E； PDBConstruct 1–100； UniProt 1–100 Author chain F； PDBConstruct 1–100； UniProt 1–100 Author chain G； PDBConstruct 1–100； UniProt 1–100 Author chain H； PDBConstruct 1–100； UniProt 1–100 Author chain I； PDBConstruct 1–100； UniProt 1–100 Author chain J； PDBConstruct 1–100； UniProt 1–100

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	2qw7
Deposition date deposition_date	2007-08-09
Structure title title	Carboxysome Subunit, CcmL
Keywords keywords	pentamer, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
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.

2qw7__assembly_1__model_1

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

Download this curve (.dat)

2qw7__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2qw7__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	22.91 Å
Rg (electron density)	21.85 Å
Total Rg	22.76 Å
Atom count	3576
Residues	479
Excluded volume	64320 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2qw7__assembly_1__model_1`	pentameric （5）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2qw7__assembly_2__model_1`	pentameric （5）	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)

Entity 1 Entity 1 polymer

Description description	Carbon dioxide concentrating mechanism protein ccmL
Molecular weight formula_weight	11935.6 kDa
Source method src_method	man
Copy count entity_count	10

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J
Atom count atom_count	7353

MQLAKVLGTVVSTSKTPNLTGVKLLLVQFLDTKGQPLERYEVAGDVVGAGLNEWVLVARGSAARKERGNGDRPLDAMVVGIIDTVNVASGSLYNKRDDGRLEAAAHHHHHH

Source Source

Source organism organism	Synechocystis sp.
NCBI taxonomy ID ncbi_taxonomy_id	1148
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	90

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6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (10 domains)

Domain ID domain_id	d2qw7a1
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.15 — EutN/CcmL-like
Family Family family	b.40.15.1 — EutN/CcmL-like

Domain ID domain_id	d2qw7b_
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.15 — EutN/CcmL-like
Family Family family	b.40.15.1 — EutN/CcmL-like

Domain ID domain_id	d2qw7c_
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.15 — EutN/CcmL-like
Family Family family	b.40.15.1 — EutN/CcmL-like

Domain ID domain_id	d2qw7d_
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.15 — EutN/CcmL-like
Family Family family	b.40.15.1 — EutN/CcmL-like

Domain ID domain_id	d2qw7e_
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.15 — EutN/CcmL-like
Family Family family	b.40.15.1 — EutN/CcmL-like

Domain ID domain_id	d2qw7f_
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.15 — EutN/CcmL-like
Family Family family	b.40.15.1 — EutN/CcmL-like

Domain ID domain_id	d2qw7g_
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.15 — EutN/CcmL-like
Family Family family	b.40.15.1 — EutN/CcmL-like

Domain ID domain_id	d2qw7h_
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.15 — EutN/CcmL-like
Family Family family	b.40.15.1 — EutN/CcmL-like

Domain ID domain_id	d2qw7i_
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.15 — EutN/CcmL-like
Family Family family	b.40.15.1 — EutN/CcmL-like

Domain ID domain_id	d2qw7j_
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.15 — EutN/CcmL-like
Family Family family	b.40.15.1 — EutN/CcmL-like

CATH v4.4 (10 domains)

Domain ID domain_id	2qw7A00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	220 — EutN/Ccml

Domain ID domain_id	2qw7B00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	220 — EutN/Ccml

Domain ID domain_id	2qw7C00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	220 — EutN/Ccml

Domain ID domain_id	2qw7D00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	220 — EutN/Ccml

Domain ID domain_id	2qw7E00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	220 — EutN/Ccml

Domain ID domain_id	2qw7F00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	220 — EutN/Ccml

Domain ID domain_id	2qw7G00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	220 — EutN/Ccml

Domain ID domain_id	2qw7H00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	220 — EutN/Ccml

Domain ID domain_id	2qw7I00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	220 — EutN/Ccml

Domain ID domain_id	2qw7J00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	220 — EutN/Ccml

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Unit-cell length a length_a	64.428 Å
Unit-cell length b length_b	107.444 Å
Unit-cell length c length_c	72.264 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	96.51 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	20

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.400 Å
Low-resolution limit resolution_low	19.900 Å
R factor r_factor	0.2430
R_work r_work	0.2400
R_free r_free	0.2960

Carboxysome Subunit, CcmL

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

Carbon dioxide concentrating mechanism protein ccmL

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

2qw7__assembly_1__model_1

2qw7__assembly_1__model_1 | I(q)

2qw7__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (10 domains)

CATH v4.4 (10 domains)

7. Citations (1)

Carboxysome Subunit, CcmL

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

Carbon dioxide concentrating mechanism protein ccmL

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

2qw7__assembly_1__model_1

2qw7__assembly_1__model_1 | I(q)

2qw7__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (10 domains)

CATH v4.4 (10 domains)

7. Citations (1)