9fu3

Closed CODH/ACS in the methylated state

Method: ELECTRON MICROSCOPY

▼

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

CO-methylating acetyl-CoA synthase

Carboxydothermus hydrogenoformans

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Carbon monoxide dehydrogenase × 1 Fe(3)-Ni(1)-S(4) cluster × 1 IRON/SULFUR CLUSTER × 3 NICKEL (II) ION × 2 SODIUM ION × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	P83789_CARHY
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–728； UniProt 5–732

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	9fu3
Deposition date deposition_date	2024-06-26
Structure title title	Closed CODH/ACS in the methylated state
Keywords keywords	CODH, ACS, CO2 fixation, reductive acetyl-CoA pathway, Wood-Ljungdahl pathway, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method method	ELECTRON MICROSCOPY

▼

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.

9fu3__assembly_1__model_1

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

Download this curve (.dat)

9fu3__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9fu3__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	39.25 Å
Rg (electron density)	39.12 Å
Total Rg	39.37 Å
Atom count	10938
Residues	1399
Excluded volume	196130 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9fu3__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 (7)

Entity 1 Entity 1 polymer

Description description	Carbon monoxide dehydrogenase
Molecular weight formula_weight	73172.1 kDa
EC 编号 ec_number	1.2.7.4
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	11224

PRFRDLEHTSKPSKADRVWEPKNRKRTIDPAALEMLEKAEKDGVKTAFDRFVEMQPQCQFGYKGLCCRFCLQGPCRLPNDDPSKKGICGASAWTIAARSVGTLILTGAAAHNEHARHIAHALKELAEGKAPDYKITDPDKLRRIAQRLGLDTQGKDDMTLAKEVAELALEDFARLPGFGENLWIKTTLNKERLEKYDECNIMPSGIFGDISDLLAQAHIGNDDDPVNITFSALRVALTDYAGMHIATDFSDVLFGTPKPIVTEANLGVLDANKVNIAVHGHNPLLSEKVVDAAKELEEEAKAAGAEGINIVGMCCTGNEVLMRRGVHLATSFASSELAIVTGAMDAVVVDVQCIMPGLKQVTECYHTRLITTSNIAKMPGTYHVPFHIENALESAKEIVRLGIEAFKQRVGKPVHIPEVKHKVVAGFSFEALMEIFAHVNQENPIRVLNDAILSGQLKGVVLFAGCNNLKRPQDESHITILKEMLKNDVFVVTTGCSAQAFAKHGFLRPEALELAGEGLKSFIKMLEEKAGLQGQLPPAFFMGSCVDNTRASDILVAMAKDLGVDTPKVPFVASAPEAMSGKAVSIGTWFVTLGVPVHVGTMPPLEGSELFYSITTQIASDVYGGYFMFEVDPVVAARKILNALEYRTWKLGVHKQTAEKFETALCQNY

Source Source

Source organism organism	Carboxydothermus hydrogenoformans Z-2901
NCBI taxonomy ID ncbi_taxonomy_id	246194
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	CO-methylating acetyl-CoA synthase
Molecular weight formula_weight	82111.2 kDa
EC 编号 ec_number	2.3.1.169
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

INFDQIFEGAIEPGKEPKRLFKEVYEGAITATSYAEILLSRAIEKYGPDHPVGYPDTAYFLPVIRAFSGEEVRTLKDMVPILNRMRAQIKSELTFENARLAGEATWYAAEIIEALRYLKHTPENPIVVPPWTGFIGDPVVRQYGIKMVDWTIPGEAIIIGRAKDSKAAKKIVDDLMGKGLMLFLCDEIIEQLLEENVKLGVDYIAYPLGNFTQVVHAANYALRAGLMFGGIAPGLRDAHRDYQRRRVLAFVLYLGEHDMVKTAAAMGAIFTGFPVITDQPLPEDKQIKDWFISEPDYDKIVQTALEVRGIKITSIDIDLPINFGPAFEGESIRKGDMHVEFGGGKTPSFELVRMVGPDEIEDGKVEVIGPDIDSVEPGGRLPIGIVVDIYGRKMQEDFEPVLERRIHYFTNYGEGFWHTAQRDLTWVRISKEAFAKGARLKHLGQLLYAKFKQEFPSIVDRVQVTIYTDEQKVLELREIARKKYAERDARLRELSDEAVDTYYSCLLCQSFAPTHVCIVSPERVGLCGAISWLDAKAAYEINPNGPNQPIPKEGLIDPVKGQWESFNEYIYKNSQRTIERMNLYTIMEYPMTSCGCFEAIMAYLPELNGFMIVNREHSGMTPIGMTFSTLAGMVGGGTQTPGFMGIGKSYIGSRKFVKADGGLARVVWMPKDLKEQLRSIIEERAEEEGLGRDFIDKIADETVGTTVDEVLPFLEEKGHPALSMEPLLRS

Source Source

Source organism organism	Carboxydothermus hydrogenoformans
NCBI taxonomy ID ncbi_taxonomy_id	129958
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	Fe(3)-Ni(1)-S(4) cluster
Molecular weight formula_weight	410.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	IRON/SULFUR CLUSTER
Molecular weight formula_weight	351.6 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 5 Entity 5 non-polymer

Description description	NICKEL (II) ION
Molecular weight formula_weight	58.7 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 6 Entity 6 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 7 Entity 7 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	286

▶

Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	—

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

Resolution resolution	2.35 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	146481

Closed CODH/ACS in the methylated state

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

CO-methylating acetyl-CoA synthase

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

9fu3__assembly_1__model_1

9fu3__assembly_1__model_1 | I(q)

9fu3__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 water

7. Citations (1)

Closed CODH/ACS in the methylated state

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

CO-methylating acetyl-CoA synthase

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

9fu3__assembly_1__model_1

9fu3__assembly_1__model_1 | I(q)

9fu3__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 water

7. Citations (1)