SAXSdb — 6qng

▼

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

Carbonic anhydrase 12

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	ZINC ION × 2 ~{N}-butyl-4-chloranyl-2-(cyclohexylamino)-5-sulfamoyl-benzamide × 2 water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	ZINC ION × 2 ~{N}-butyl-4-chloranyl-2-(cyclohexylamino)-5-sulfamoyl-benzamide × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CAH12_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–263； UniProt 30–291 Author chain B； PDBConstruct 2–263； UniProt 30–291 Author chain C； PDBConstruct 2–263； UniProt 30–291 Author chain D； PDBConstruct 2–263； UniProt 30–291

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_id	6qng
Deposition date deposition_date	2019-02-11
Structure title title	Three dimensional structure of human carbonic anhydrase XII in complex with benzenesulfonamide
Keywords keywords	LYASE; LYASE
Experimental Method method	X-RAY DIFFRACTION

▼

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.

6qng__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

6qng__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

6qng__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	25.46 Å
Rg (electron density)	24.78 Å
Total Rg	25.56 Å
Atom count	4224
Residues	520
Excluded volume	74410 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`6qng__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`6qng__assembly_2__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 (4)

Entity 1 Entity 1 polymer

Description description	Carbonic anhydrase 12
Molecular weight formula_weight	29857.2 kDa
EC 编号 ec_number	4.2.1.1
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	9279

ASKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQGLQSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFSHLQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPREMINNFRQVQKFDERLVYTSFSQ

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 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 non-polymer

Description description	~{N}-butyl-4-chloranyl-2-(cyclohexylamino)-5-sulfamoyl-benzamide
Molecular weight formula_weight	387.9 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	827

▼

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d6qnga_
Class class	b — All beta proteins
Fold Fold fold	b.74 — Carbonic anhydrase
Superfamily Superfamily superfamily	b.74.1 — Carbonic anhydrase
Family Family family	b.74.1.1 — Carbonic anhydrase

Domain ID domain_id	d6qngb_
Class class	b — All beta proteins
Fold Fold fold	b.74 — Carbonic anhydrase
Superfamily Superfamily superfamily	b.74.1 — Carbonic anhydrase
Family Family family	b.74.1.1 — Carbonic anhydrase

Domain ID domain_id	d6qngc_
Class class	b — All beta proteins
Fold Fold fold	b.74 — Carbonic anhydrase
Superfamily Superfamily superfamily	b.74.1 — Carbonic anhydrase
Family Family family	b.74.1.1 — Carbonic anhydrase

Domain ID domain_id	d6qngd_
Class class	b — All beta proteins
Fold Fold fold	b.74 — Carbonic anhydrase
Superfamily Superfamily superfamily	b.74.1 — Carbonic anhydrase
Family Family family	b.74.1.1 — Carbonic anhydrase

CATH v4.4 (4 domains)

Domain ID domain_id	6qngA00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	200 — Carbonic Anhydrase II
Homologous superfamily homologous superfamily	10 — Alpha carbonic anhydrase

Domain ID domain_id	6qngB00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	200 — Carbonic Anhydrase II
Homologous superfamily homologous superfamily	10 — Alpha carbonic anhydrase

Domain ID domain_id	6qngC00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	200 — Carbonic Anhydrase II
Homologous superfamily homologous superfamily	10 — Alpha carbonic anhydrase

Domain ID domain_id	6qngD00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	200 — Carbonic Anhydrase II
Homologous superfamily homologous superfamily	10 — Alpha carbonic anhydrase

▶

Unit-cell length a length_a	46.930 Å
Unit-cell length b length_b	66.050 Å
Unit-cell length c length_c	80.950 Å
Unit-cell angle α angle_alpha	82.09 °
Unit-cell angle β angle_beta	84.41 °
Unit-cell angle γ angle_gamma	86.17 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	1.670 Å
Low-resolution limit resolution_low	65.330 Å
R factor r_factor	0.1952
R_work r_work	0.1924
R_free r_free	0.2497

Three dimensional structure of human carbonic anhydrase XII in complex with benzenesulfonamide

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

Carbonic anhydrase 12

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

6qng__assembly_2__model_1

6qng__assembly_2__model_1 | I(q)

6qng__assembly_2__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Three dimensional structure of human carbonic anhydrase XII in complex with benzenesulfonamide

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

Carbonic anhydrase 12

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

6qng__assembly_2__model_1

6qng__assembly_2__model_1 | I(q)

6qng__assembly_2__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)