3i01

Native structure of bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase from Moorella thermoacetica, water-bound C-cluster.

Method: X-RAY DIFFRACTION

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

Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit beta

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit alpha × 2 （P27988） IRON/SULFUR CLUSTER × 5 FE(4)-NI(1)-S(4) CLUSTER × 2 GLYCEROL × 2 COPPER (I) ION × 2 NICKEL (II) ION × 2 ACETATE ION × 2 SODIUM ION × 2 water × 4	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 4	Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit alpha × 2 （P27988） IRON/SULFUR CLUSTER × 5 FE(4)-NI(1)-S(4) CLUSTER × 2 GLYCEROL × 2 COPPER (I) ION × 2 NICKEL (II) ION × 2 ACETATE ION × 2 SODIUM ION × 2 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	DCMB_MOOTH
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–674； UniProt 1–674 Author chain B； PDBConstruct 1–674； UniProt 1–674 Author chain C； PDBConstruct 1–674； UniProt 1–674 Author chain D； PDBConstruct 1–674； UniProt 1–674

Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit alpha

OrganismNot specified

UniProt P27988

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit beta × 2 （P27989） IRON/SULFUR CLUSTER × 5 FE(4)-NI(1)-S(4) CLUSTER × 2 GLYCEROL × 2 COPPER (I) ION × 2 NICKEL (II) ION × 2 ACETATE ION × 2 SODIUM ION × 2 water × 4	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 4	Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit beta × 2 （P27989） IRON/SULFUR CLUSTER × 5 FE(4)-NI(1)-S(4) CLUSTER × 2 GLYCEROL × 2 COPPER (I) ION × 2 NICKEL (II) ION × 2 ACETATE ION × 2 SODIUM ION × 2 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	DCMA_MOOTH
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain M； PDBConstruct 1–729； UniProt 1–729 Author chain N； PDBConstruct 1–729； UniProt 1–729 Author chain O； PDBConstruct 1–729； UniProt 1–729 Author chain P； PDBConstruct 1–729； UniProt 1–729

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	3i01
Deposition date deposition_date	2009-06-24
Structure title title	Native structure of bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase from Moorella thermoacetica, water-bound C-cluster.
Keywords keywords	;protein-protein complex, Carbon dioxide fixation, Electron transport, Iron, Iron-sulfur, Metal-binding, Nickel, Oxidoreductase, Transport, Transferase, OXIDOREDUCTASE-TRANSFERASE COMPLEX ;; OXIDOREDUCTASE/TRANSFERASE
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.

3i01__assembly_1__model_1

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

Download this curve (.dat)

3i01__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3i01__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	51.32 Å
Rg (electron density)	52.08 Å
Total Rg	51.76 Å
Atom count	21740
Residues	2802
Excluded volume	389330 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3i01__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3i01__assembly_2__model_1`	tetrameric （4）	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 (10)

Entity 1 Entity 1 polymer

Description description	Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit beta
Molecular weight formula_weight	73006.9 kDa
EC 编号 ec_number	1.2.7.4, 1.2.99.2
Source method src_method	nat
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	45096

MPRFRDLSHNCRPSEAPRVMEPKNRDRTVDPAVLEMLVKSKDDKVITAFDRFVAQQPQCKIGYEGICCRFCMAGPCRIKATDGPGSRGICGASAWTIVARNVGLMILTGAAAHCEHGNHIAHALVEMAEGKAPDYSVKDEAKLKEVCRRVGIEVEGKSVLELAQEVGEKALEDFRRLKGEGEATWLMTTINEGRKEKFRTHNVVPFGIHASISELVNQAHMGMDNDPVNLVFSAIRVALADYTGEHIATDFSDILFGTPQPVVSEANMGVLDPDQVNFVLHGHNPLLSEIIVQAAREMEGEAKAAGAKGINLVGICCTGNEVLMRQGIPLVTSFASQELAICTGAIDAMCVDVQCIMPSISAVAECYHTRIITTADNAKIPGAYHIDYQTATAIESAKTAIRMAIEAFKERKESNRPVYIPQIKNRVVAGWSLEALTKLLATQNAQNPIRVLNQAILDGELAGVALICGCNNLKGFQDNSHLTVMKELLKNNVFVVATGCSAQAAGKLGLLDPANVETYCGDGLKGFLKRLGEGANIEIGLPPVFHMGSCVDNSRAVDLLMAMANDLGVDTPKVPFVASAPEAMSGKAAAIGTWWVSLGVPTHVGTMPPVEGSDLIYSILTQIASDVYGGYFIFEMDPQVAARKILDALEYRTWKLGVHKEVAERYETKLCQGY

Entity 2 Entity 2 polymer

Description description	Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit alpha
Molecular weight formula_weight	81816.9 kDa
EC 编号 ec_number	2.3.1.169
Source method src_method	nat
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	M,N,O,P

MTDFDKIFEGAIPEGKEPVALFREVYHGAITATSYAEILLNQAIRTYGPDHPVGYPDTAYYLPVIRCFSGEEVKKLGDLPPILNRKRAQVSPVLNFENARLAGEATWYAAEIIEALRYLKYKPDEPLLPPPWTGFIGDPVVRRFGIKMVDWTIPGEAIILGRAKDSKALAKIVKELMGMGFMLFICDEAVEQLLEENVKLGIDYIAYPLGNFTQIVHAANYALRAGMMFGGVTPGAREEQRDYQRRRIRAFVLYLGEHDMVKTAAAFGAIFTGFPVITDQPLPEDKQIPDWFFSVEDYDKIVQIAMETRGIKLTKIKLDLPINFGPAFEGESIRKGDMYVEMGGNRTPAFELVRTVSESEITDGKIEVIGPDIDQIPEGSKLPLGILVDIYGRKMQADFEGVLERRIHDFINYGEGLWHTGQRNINWLRVSKDAVAKGFRFKNYGEILVAKMKEEFPAIVDRVQVTIFTDEAKVKEYMEVAREKYKERDDRMRGLTDETVDTFYSCVLCQSFAPNHVCIVTPERVGLCGAVSWLDAKASYEINHAGPNQPIPKEGEIDPIKGIWKSVNDYLYTASNRNLEQVCLYTLMENPMTSCGCFEAIMAILPECNGIMITTRDHAGMTPSGMTFSTLAGMIGGGTQTPGFMGIGRTYIVSKKFISADGGIARIVWMPKSLKDFLHDEFVRRSVEEGLGEDFIDKIADETIGTTVDEILPYLEEKGHPALTMDPIM

Entity 3 Entity 3 non-polymer

Description description	IRON/SULFUR CLUSTER
Molecular weight formula_weight	351.6 kDa
Source method src_method	syn
Copy count entity_count	10

Entity 4 Entity 4 non-polymer

Description description	FE(4)-NI(1)-S(4) CLUSTER
Molecular weight formula_weight	410.3 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 5 Entity 5 non-polymer

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

Entity 6 Entity 6 non-polymer

Description description	COPPER (I) ION
Molecular weight formula_weight	63.5 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 7 Entity 7 non-polymer

Description description	NICKEL (II) ION
Molecular weight formula_weight	58.7 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 8 Entity 8 non-polymer

Description description	ACETATE ION
Molecular weight formula_weight	59.0 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 9 Entity 9 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 10 Entity 10 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1413

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6. Fold Classification (SCOP + CATH) 40 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d3i01a_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.26 — Prismane protein-like
Superfamily Superfamily superfamily	e.26.1 — Prismane protein-like
Family Family family	e.26.1.2 — Carbon monoxide dehydrogenase

Domain ID domain_id	d3i01b_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.26 — Prismane protein-like
Superfamily Superfamily superfamily	e.26.1 — Prismane protein-like
Family Family family	e.26.1.2 — Carbon monoxide dehydrogenase

Domain ID domain_id	d3i01c_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.26 — Prismane protein-like
Superfamily Superfamily superfamily	e.26.1 — Prismane protein-like
Family Family family	e.26.1.2 — Carbon monoxide dehydrogenase

Domain ID domain_id	d3i01d_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.26 — Prismane protein-like
Superfamily Superfamily superfamily	e.26.1 — Prismane protein-like
Family Family family	e.26.1.2 — Carbon monoxide dehydrogenase

Domain ID domain_id	d3i01m_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.26 — Prismane protein-like
Superfamily Superfamily superfamily	e.26.1 — Prismane protein-like
Family Family family	e.26.1.3 — Acetyl-CoA synthase

Domain ID domain_id	d3i01n_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.26 — Prismane protein-like
Superfamily Superfamily superfamily	e.26.1 — Prismane protein-like
Family Family family	e.26.1.3 — Acetyl-CoA synthase

Domain ID domain_id	d3i01o_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.26 — Prismane protein-like
Superfamily Superfamily superfamily	e.26.1 — Prismane protein-like
Family Family family	e.26.1.3 — Acetyl-CoA synthase

Domain ID domain_id	d3i01p_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.26 — Prismane protein-like
Superfamily Superfamily superfamily	e.26.1 — Prismane protein-like
Family Family family	e.26.1.3 — Acetyl-CoA synthase

CATH v4.4 (32 domains)

Domain ID domain_id	3i01A01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1270 — Substrate Binding Domain Of Dnak; Chain:A; Domain 2
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3i01A02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	2030 —

Domain ID domain_id	3i01A03
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	2030 —

Domain ID domain_id	3i01B01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1270 — Substrate Binding Domain Of Dnak; Chain:A; Domain 2
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3i01B02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	2030 —

Domain ID domain_id	3i01B03
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	2030 —

Domain ID domain_id	3i01C01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1270 — Substrate Binding Domain Of Dnak; Chain:A; Domain 2
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3i01C02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	2030 —

Domain ID domain_id	3i01C03
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	2030 —

Domain ID domain_id	3i01D01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1270 — Substrate Binding Domain Of Dnak; Chain:A; Domain 2
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3i01D02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	2030 —

Domain ID domain_id	3i01D03
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	2030 —

Domain ID domain_id	3i01M01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily	190 — Carbon monoxide dehydrogenase alpha subunit. Chain M, domain 1

Domain ID domain_id	3i01M02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	2030 —

Domain ID domain_id	3i01M03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1650 — Bifunctional carbon monoxide dehydrogenase/acetyl-coa synthase(codh/acs), Chain M, domain 3
Homologous superfamily homologous superfamily	10 — Bifunctional carbon monoxide dehydrogenase/acetyl-coa synthase(codh/acs), Chain M, domain 3

Domain ID domain_id	3i01M04
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	970 — Ribonuclease HI; Chain A
Homologous superfamily homologous superfamily	20 — Carbon monoxide dehydrogenase alpha subunit. Chain D, domain 4

Domain ID domain_id	3i01M05
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1470 — Bifunctional carbon monoxide dehydrogenase/acetyl-coa synthase(codh/acs), Chain M, domain 5
Homologous superfamily homologous superfamily	10 — Bifunctional carbon monoxide dehydrogenase/acetyl-coa synthase(codh/acs), Chain M, domain 5

Domain ID domain_id	3i01N01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily	190 — Carbon monoxide dehydrogenase alpha subunit. Chain M, domain 1

Domain ID domain_id	3i01N02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	2030 —

Domain ID domain_id	3i01N03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1650 — Bifunctional carbon monoxide dehydrogenase/acetyl-coa synthase(codh/acs), Chain M, domain 3
Homologous superfamily homologous superfamily	10 — Bifunctional carbon monoxide dehydrogenase/acetyl-coa synthase(codh/acs), Chain M, domain 3

Domain ID domain_id	3i01N04
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	970 — Ribonuclease HI; Chain A
Homologous superfamily homologous superfamily	20 — Carbon monoxide dehydrogenase alpha subunit. Chain D, domain 4

Domain ID domain_id	3i01N05
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1470 — Bifunctional carbon monoxide dehydrogenase/acetyl-coa synthase(codh/acs), Chain M, domain 5
Homologous superfamily homologous superfamily	10 — Bifunctional carbon monoxide dehydrogenase/acetyl-coa synthase(codh/acs), Chain M, domain 5

Domain ID domain_id	3i01O01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily	190 — Carbon monoxide dehydrogenase alpha subunit. Chain M, domain 1

Domain ID domain_id	3i01O02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	2030 —

Domain ID domain_id	3i01O03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1650 — Bifunctional carbon monoxide dehydrogenase/acetyl-coa synthase(codh/acs), Chain M, domain 3
Homologous superfamily homologous superfamily	10 — Bifunctional carbon monoxide dehydrogenase/acetyl-coa synthase(codh/acs), Chain M, domain 3

Domain ID domain_id	3i01O04
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	970 — Ribonuclease HI; Chain A
Homologous superfamily homologous superfamily	20 — Carbon monoxide dehydrogenase alpha subunit. Chain D, domain 4

Domain ID domain_id	3i01O05
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1470 — Bifunctional carbon monoxide dehydrogenase/acetyl-coa synthase(codh/acs), Chain M, domain 5
Homologous superfamily homologous superfamily	10 — Bifunctional carbon monoxide dehydrogenase/acetyl-coa synthase(codh/acs), Chain M, domain 5

Domain ID domain_id	3i01P01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily	190 — Carbon monoxide dehydrogenase alpha subunit. Chain M, domain 1

Domain ID domain_id	3i01P02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	2030 —

Domain ID domain_id	3i01P03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1650 — Bifunctional carbon monoxide dehydrogenase/acetyl-coa synthase(codh/acs), Chain M, domain 3
Homologous superfamily homologous superfamily	10 — Bifunctional carbon monoxide dehydrogenase/acetyl-coa synthase(codh/acs), Chain M, domain 3

Domain ID domain_id	3i01P04
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	970 — Ribonuclease HI; Chain A
Homologous superfamily homologous superfamily	20 — Carbon monoxide dehydrogenase alpha subunit. Chain D, domain 4

Domain ID domain_id	3i01P05
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1470 — Bifunctional carbon monoxide dehydrogenase/acetyl-coa synthase(codh/acs), Chain M, domain 5
Homologous superfamily homologous superfamily	10 — Bifunctional carbon monoxide dehydrogenase/acetyl-coa synthase(codh/acs), Chain M, domain 5

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Unit-cell length a length_a	99.651 Å
Unit-cell length b length_b	136.870 Å
Unit-cell length c length_c	140.864 Å
Unit-cell angle α angle_alpha	101.26 °
Unit-cell angle β angle_beta	109.11 °
Unit-cell angle γ angle_gamma	104.08 °
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	2.150 Å
Low-resolution limit resolution_low	36.960 Å
R factor r_factor	0.1890
R_work r_work	0.1863
R_free r_free	0.2415

Native structure of bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase from Moorella thermoacetica, water-bound C-cluster.

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

Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit beta

State in the Current Structure

Other States of the Same Protein in the Database

Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit alpha

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

3i01__assembly_1__model_1

3i01__assembly_1__model_1 | I(q)

3i01__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 (10)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

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 non-polymer

Entity 8 Entity 8 non-polymer

Entity 9 Entity 9 non-polymer

Entity 10 Entity 10 water

6. Fold Classification (SCOP + CATH) 40 domains

SCOP 2.08 (8 domains)

CATH v4.4 (32 domains)

7. Citations (1)

Native structure of bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase from Moorella thermoacetica, water-bound C-cluster.

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

Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit beta

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit alpha

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

3i01__assembly_1__model_1

3i01__assembly_1__model_1 | I(q)

3i01__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 (10)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

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 non-polymer

Entity 8 Entity 8 non-polymer

Entity 9 Entity 9 non-polymer

Entity 10 Entity 10 water

6. Fold Classification (SCOP + CATH) 40 domains

SCOP 2.08 (8 domains)

CATH v4.4 (32 domains)

7. Citations (1)