1oao

NiZn[Fe4S4] and NiNi[Fe4S4] clusters in closed and open alpha subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase

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 FORMYL GROUP × 2 SULFATE ION × 31 GLYCEROL × 8 FE (II) ION × 2 BICARBONATE ION × 1 ZINC ION × 1 NICKEL (II) ION × 3 SULFUR OXIDE × 1 ACETATE ION × 1 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

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 FORMYL GROUP × 2 SULFATE ION × 31 GLYCEROL × 8 FE (II) ION × 2 BICARBONATE ION × 1 ZINC ION × 1 NICKEL (II) ION × 3 SULFUR OXIDE × 1 ACETATE ION × 1 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 C； PDBConstruct 1–729； UniProt 1–729 Author chain D； 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	1oao
Deposition date deposition_date	2003-01-20
Structure title title	NiZn[Fe4S4] and NiNi[Fe4S4] clusters in closed and open alpha subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase
Keywords keywords	OXIDOREDUCTASE-TRANSFERASE COMPLEX, ELECTRON TRANSFER, OXIDOREDUCTASE, ACETYL-COA FORMATION, WOOD/LJUNGDAHL PATHWAY, NICKEL; 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.

1oao__assembly_1__model_1

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

Download this curve (.dat)

1oao__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1oao__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	52.34 Å
Rg (electron density)	53.34 Å
Total Rg	52.96 Å
Atom count	21955
Residues	2803
Excluded volume	392200 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1oao__assembly_1__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 (14)

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	1.2.99.2, 1.2.7.4
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	23346

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	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D

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	5

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	2

Entity 5 Entity 5 non-polymer

Description description	FORMYL GROUP
Molecular weight formula_weight	30.0 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 6 Entity 6 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	31

Entity 7 Entity 7 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 8 Entity 8 non-polymer

Description description	FE (II) ION
Molecular weight formula_weight	55.8 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 9 Entity 9 non-polymer

Description description	BICARBONATE ION
Molecular weight formula_weight	61.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 10 Entity 10 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 11 Entity 11 non-polymer

Description description	NICKEL (II) ION
Molecular weight formula_weight	58.7 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 12 Entity 12 non-polymer

Description description	SULFUR OXIDE
Molecular weight formula_weight	48.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 13 Entity 13 non-polymer

Description description	ACETATE ION
Molecular weight formula_weight	59.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 14 Entity 14 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1271

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6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1oaoa_
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	d1oaob_
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	d1oaoc_
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	d1oaod_
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 (16 domains)

Domain ID domain_id	1oaoA01
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	1oaoA02
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	1oaoA03
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	1oaoB01
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	1oaoB02
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	1oaoB03
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	1oaoC01
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	1oaoC02
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	1oaoC03
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	1oaoC04
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	1oaoC05
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	1oaoD01
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	1oaoD02
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	1oaoD03
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	1oaoD04
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	1oaoD05
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	244.570 Å
Unit-cell length b length_b	81.890 Å
Unit-cell length c length_c	167.220 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	96.19 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	25.000 Å
R factor r_factor	0.1490
R_work r_work	0.1470
R_free r_free	0.1790

NiZn[Fe4S4] and NiNi[Fe4S4] clusters in closed and open alpha subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase

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

1oao__assembly_1__model_1

1oao__assembly_1__model_1 | I(q)

1oao__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 (14)

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 non-polymer

Entity 11 Entity 11 non-polymer

Entity 12 Entity 12 non-polymer

Entity 13 Entity 13 non-polymer

Entity 14 Entity 14 water

6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (4 domains)

CATH v4.4 (16 domains)

7. Citations (1)

NiZn[Fe4S4] and NiNi[Fe4S4] clusters in closed and open alpha subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase

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

1oao__assembly_1__model_1

1oao__assembly_1__model_1 | I(q)

1oao__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 (14)

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 non-polymer

Entity 11 Entity 11 non-polymer

Entity 12 Entity 12 non-polymer

Entity 13 Entity 13 non-polymer

Entity 14 Entity 14 water

6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (4 domains)

CATH v4.4 (16 domains)

7. Citations (1)