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9tdm

Cryo-EM structure of AccA3/AccD4/AccD5/AccE5 in complex with Propionyl-CoA

Method: ELECTRON MICROSCOPY Dmax: 215.7 Å Quality: GOOD
▼

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

Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit

OrganismNot specified

UniProt A0QTE1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 16 PDB declaration: 16-meric（16） Consistent with protein copy count Chain A3a； UniProt 1–598 Chain A3b； UniProt 1–598 Chain A3c； UniProt 1–598 Chain A3d； UniProt 1–598 Chain A3e； UniProt 1–598 Chain A3f； UniProt 1–598 Chain A3g； UniProt 1–598 Chain A3h； UniProt 1–598 Not recorded Propionyl-CoA carboxylase beta chain × 2 （A0R616） Propionyl-CoA carboxylase beta chain × 4 （A0QTE7） Acetyl-/propionyl-coenzyme A carboxylase AccE5 × 2 （A0QTE6） ADENOSINE-5'-TRIPHOSPHATE × 2 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL × 5 propionyl Coenzyme A × 4 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 2.40 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 9TDM Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
30HU cryo-EM structure of AccA3-AccE5 complex in the presence of Arachidyl-CoA Deposited 2026-04-27 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain A3a 1–598（598 aa）
Chain A3b 1–598（598 aa）
Chain A3c 1–598（598 aa）
Chain A3d 1–598（598 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 3.50 Å
9T97 cryo-EM structure of AccA3/AccD4/AccD5/AccE5 complex from Mycobacterium smegmatis Deposited 2025-11-14 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: 15-meric
Chain A3a 1–598（598 aa）
Chain A3b 1–598（598 aa）
Chain A3c 1–598（598 aa）
Chain A3d 1–598（598 aa）
Chain A3f 1–598（598 aa）
Chain A3g 1–598（598 aa）
Chain A3i 1–598（598 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 2.35 Å
9YX1 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis Deposited 2025-10-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric
Chain A 1–598（598 aa）
Chain B 1–598（598 aa）
Chain C 1–598（598 aa）
Chain D 1–598（598 aa）
Chain I 1–598（598 aa）
Chain J 1–598（598 aa）
Chain K 1–598（598 aa）
Chain L 1–598（598 aa）
Chain Q 1–598（598 aa）
Chain R 1–598（598 aa）
Chain S 1–598（598 aa）
Chain T 1–598（598 aa）
Not recorded BTN BIOTIN × 6 BCT BICARBONATE ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å
9YX2 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with ATP, bicarbonate, and propionyl-CoA Deposited 2025-10-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric
Chain A 1–598（598 aa）
Chain B 1–598（598 aa）
Chain C 1–598（598 aa）
Chain D 1–598（598 aa）
Chain I 1–598（598 aa）
Chain J 1–598（598 aa）
Chain K 1–598（598 aa）
Chain L 1–598（598 aa）
Chain Q 1–598（598 aa）
Chain R 1–598（598 aa）
Chain S 1–598（598 aa）
Chain T 1–598（598 aa）
Not recorded BTN BIOTIN × 6 BCT BICARBONATE ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 8 MG MAGNESIUM ION × 8 1VU propionyl Coenzyme A × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
9YX4 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with ATP, bicarbonate, arachidoyl-CoA, and propionyl-CoA Deposited 2025-10-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric
Chain A 1–598（598 aa）
Chain B 1–598（598 aa）
Chain C 1–598（598 aa）
Chain D 1–598（598 aa）
Chain I 1–598（598 aa）
Chain J 1–598（598 aa）
Chain K 1–598（598 aa）
Chain L 1–598（598 aa）
Chain Q 1–598（598 aa）
Chain R 1–598（598 aa）
Chain S 1–598（598 aa）
Chain T 1–598（598 aa）
Not recorded BTN BIOTIN × 6 BCT BICARBONATE ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 8 MG MAGNESIUM ION × 8 A1CZD S-{(3S,5S,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5,10,14-tetraoxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (11E,14E,16E)-icosa-11,14,16-trienethioate (non-preferred name) × 2 1VU propionyl Coenzyme A × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.30 Å
9YX5 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with MSMEG_0435-MSMEG_0436 bound Deposited 2025-10-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 26 PDB declaration: 26-meric
Chain A 1–598（598 aa）
Chain B 1–598（598 aa）
Chain C 1–598（598 aa）
Chain D 1–598（598 aa）
Chain I 1–598（598 aa）
Chain J 1–598（598 aa）
Chain K 1–598（598 aa）
Chain L 1–598（598 aa）
Chain Q 1–598（598 aa）
Chain R 1–598（598 aa）
Chain S 1–598（598 aa）
Chain T 1–598（598 aa）
Chain U 1–598（598 aa）
Chain X 1–598（598 aa）
Not recorded A1CZD S-{(3S,5S,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5,10,14-tetraoxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (11E,14E,16E)-icosa-11,14,16-trienethioate (non-preferred name) × 2 1VU propionyl Coenzyme A × 4 BTN BIOTIN × 5 BCT BICARBONATE ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0QTE1_MYCS2
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A3a； PDBConstruct 1–598； UniProt 1–598 Author chain A3b； PDBConstruct 1–598； UniProt 1–598 Author chain A3c； PDBConstruct 1–598； UniProt 1–598 Author chain A3d； PDBConstruct 1–598； UniProt 1–598 Author chain A3e； PDBConstruct 1–598； UniProt 1–598 Author chain A3f； PDBConstruct 1–598； UniProt 1–598 Author chain A3g； PDBConstruct 1–598； UniProt 1–598 Author chain A3h； PDBConstruct 1–598； UniProt 1–598

Propionyl-CoA carboxylase beta chain

OrganismNot specified

UniProt A0R616

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 16 PDB declaration: 16-meric（16） Consistent with protein copy count Chain D4a； UniProt 1–517 Chain D4b； UniProt 1–517 Not recorded Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit × 8 （A0QTE1） Propionyl-CoA carboxylase beta chain × 4 （A0QTE7） Acetyl-/propionyl-coenzyme A carboxylase AccE5 × 2 （A0QTE6） ADENOSINE-5'-TRIPHOSPHATE × 2 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL × 5 propionyl Coenzyme A × 4 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 2.40 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 9TDM Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
9T97 cryo-EM structure of AccA3/AccD4/AccD5/AccE5 complex from Mycobacterium smegmatis Deposited 2025-11-14 Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: 15-meric
Chain D4a 1–517（517 aa）
Chain D4b 1–517（517 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 2.35 Å
9YX1 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis Deposited 2025-10-26 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric
Chain F 1–517（517 aa）
Chain O 1–517（517 aa）
Not recorded BTN BIOTIN × 6 BCT BICARBONATE ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å
9YX2 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with ATP, bicarbonate, and propionyl-CoA Deposited 2025-10-26 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric
Chain F 1–517（517 aa）
Chain O 1–517（517 aa）
Not recorded BTN BIOTIN × 6 BCT BICARBONATE ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 8 MG MAGNESIUM ION × 8 1VU propionyl Coenzyme A × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
9YX4 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with ATP, bicarbonate, arachidoyl-CoA, and propionyl-CoA Deposited 2025-10-26 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric
Chain F 1–517（517 aa）
Chain O 1–517（517 aa）
Not recorded BTN BIOTIN × 6 BCT BICARBONATE ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 8 MG MAGNESIUM ION × 8 A1CZD S-{(3S,5S,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5,10,14-tetraoxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (11E,14E,16E)-icosa-11,14,16-trienethioate (non-preferred name) × 2 1VU propionyl Coenzyme A × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.30 Å
9YX5 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with MSMEG_0435-MSMEG_0436 bound Deposited 2025-10-26 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 26 PDB declaration: 26-meric
Chain F 1–517（517 aa）
Chain O 1–517（517 aa）
Not recorded A1CZD S-{(3S,5S,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5,10,14-tetraoxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (11E,14E,16E)-icosa-11,14,16-trienethioate (non-preferred name) × 2 1VU propionyl Coenzyme A × 4 BTN BIOTIN × 5 BCT BICARBONATE ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0R616_MYCS2
Isoform —
PDB entities 2
Chains and sequence ranges Author chain D4a； PDBConstruct 1–517； UniProt 1–517 Author chain D4b； PDBConstruct 1–517； UniProt 1–517

Propionyl-CoA carboxylase beta chain

OrganismNot specified

UniProt A0QTE7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 16 PDB declaration: 16-meric（16） Consistent with protein copy count Chain D5a； UniProt 1–542 Chain D5b； UniProt 1–542 Chain D5c； UniProt 1–542 Chain D5d； UniProt 1–542 Not recorded Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit × 8 （A0QTE1） Propionyl-CoA carboxylase beta chain × 2 （A0R616） Acetyl-/propionyl-coenzyme A carboxylase AccE5 × 2 （A0QTE6） ADENOSINE-5'-TRIPHOSPHATE × 2 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL × 5 propionyl Coenzyme A × 4 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 2.40 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 9TDM Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
9T97 cryo-EM structure of AccA3/AccD4/AccD5/AccE5 complex from Mycobacterium smegmatis Deposited 2025-11-14 Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: 15-meric
Chain D5a 1–542（542 aa）
Chain D5b 1–542（542 aa）
Chain D5c 1–542（542 aa）
Chain D5d 1–542（542 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 2.35 Å
9YX1 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis Deposited 2025-10-26 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric
Chain G 1–542（542 aa）
Chain H 1–542（542 aa）
Chain M 1–542（542 aa）
Chain N 1–542（542 aa）
Not recorded BTN BIOTIN × 6 BCT BICARBONATE ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å
9YX2 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with ATP, bicarbonate, and propionyl-CoA Deposited 2025-10-26 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric
Chain G 1–542（542 aa）
Chain H 1–542（542 aa）
Chain M 1–542（542 aa）
Chain N 1–542（542 aa）
Not recorded BTN BIOTIN × 6 BCT BICARBONATE ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 8 MG MAGNESIUM ION × 8 1VU propionyl Coenzyme A × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
9YX4 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with ATP, bicarbonate, arachidoyl-CoA, and propionyl-CoA Deposited 2025-10-26 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric
Chain G 1–542（542 aa）
Chain H 1–542（542 aa）
Chain M 1–542（542 aa）
Chain N 1–542（542 aa）
Not recorded BTN BIOTIN × 6 BCT BICARBONATE ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 8 MG MAGNESIUM ION × 8 A1CZD S-{(3S,5S,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5,10,14-tetraoxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (11E,14E,16E)-icosa-11,14,16-trienethioate (non-preferred name) × 2 1VU propionyl Coenzyme A × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.30 Å
9YX5 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with MSMEG_0435-MSMEG_0436 bound Deposited 2025-10-26 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 26 PDB declaration: 26-meric
Chain G 1–542（542 aa）
Chain H 1–542（542 aa）
Chain M 1–542（542 aa）
Chain N 1–542（542 aa）
Not recorded A1CZD S-{(3S,5S,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5,10,14-tetraoxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (11E,14E,16E)-icosa-11,14,16-trienethioate (non-preferred name) × 2 1VU propionyl Coenzyme A × 4 BTN BIOTIN × 5 BCT BICARBONATE ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0QTE7_MYCS2
Isoform —
PDB entities 3
Chains and sequence ranges Author chain D5a； PDBConstruct 1–542； UniProt 1–542 Author chain D5b； PDBConstruct 1–542； UniProt 1–542 Author chain D5c； PDBConstruct 1–542； UniProt 1–542 Author chain D5d； PDBConstruct 1–542； UniProt 1–542

Acetyl-/propionyl-coenzyme A carboxylase AccE5

OrganismNot specified

UniProt A0QTE6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 16 PDB declaration: 16-meric（16） Consistent with protein copy count Chain E5a； UniProt 1–94 Chain E5b； UniProt 1–94 Not recorded Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit × 8 （A0QTE1） Propionyl-CoA carboxylase beta chain × 2 （A0R616） Propionyl-CoA carboxylase beta chain × 4 （A0QTE7） ADENOSINE-5'-TRIPHOSPHATE × 2 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL × 5 propionyl Coenzyme A × 4 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 2.40 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 9TDM Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
30HU cryo-EM structure of AccA3-AccE5 complex in the presence of Arachidyl-CoA Deposited 2026-04-27 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain E5a 1–94（94 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 3.50 Å
9T97 cryo-EM structure of AccA3/AccD4/AccD5/AccE5 complex from Mycobacterium smegmatis Deposited 2025-11-14 Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: 15-meric
Chain E5a 1–94（94 aa）
Chain E5b 1–94（94 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 2.35 Å
9YX1 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis Deposited 2025-10-26 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric
Chain E 1–94（94 aa）
Chain P 1–94（94 aa）
Not recorded BTN BIOTIN × 6 BCT BICARBONATE ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å
9YX2 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with ATP, bicarbonate, and propionyl-CoA Deposited 2025-10-26 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric
Chain E 1–94（94 aa）
Chain P 1–94（94 aa）
Not recorded BTN BIOTIN × 6 BCT BICARBONATE ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 8 MG MAGNESIUM ION × 8 1VU propionyl Coenzyme A × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
9YX4 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with ATP, bicarbonate, arachidoyl-CoA, and propionyl-CoA Deposited 2025-10-26 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric
Chain E 1–94（94 aa）
Chain P 1–94（94 aa）
Not recorded BTN BIOTIN × 6 BCT BICARBONATE ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 8 MG MAGNESIUM ION × 8 A1CZD S-{(3S,5S,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5,10,14-tetraoxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (11E,14E,16E)-icosa-11,14,16-trienethioate (non-preferred name) × 2 1VU propionyl Coenzyme A × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.30 Å
9YX5 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with MSMEG_0435-MSMEG_0436 bound Deposited 2025-10-26 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 26 PDB declaration: 26-meric
Chain E 1–94（94 aa）
Chain P 1–94（94 aa）
Not recorded A1CZD S-{(3S,5S,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5,10,14-tetraoxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (11E,14E,16E)-icosa-11,14,16-trienethioate (non-preferred name) × 2 1VU propionyl Coenzyme A × 4 BTN BIOTIN × 5 BCT BICARBONATE ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0QTE6_MYCS2
Isoform —
PDB entities 4
Chains and sequence ranges Author chain E5a； PDBConstruct 1–94； UniProt 1–94 Author chain E5b； PDBConstruct 1–94； UniProt 1–94

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.

SAXS scattering curve SAXS Profile

SAXS profile for 9tdm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9tdm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9tdm
Deposition date deposition_date2025-11-24
Structure title titleCryo-EM structure of AccA3/AccD4/AccD5/AccE5 in complex with Propionyl-CoA
Keywords keywordsBio-dependent acyl-CoA carboxylase, long chain/short chain acyl-CoA carboxylase, TRANSFERASE; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier76.44 Å
Radius of gyration Rg (electron density) rg_electron76.40 Å
Forward intensity I(0) i09578150000.00
Molecular weight molecular_weight823190.0 kDa
Excluded volume excluded_volume1028400 ų
Envelope volume envelope_volume1767400 ų
Hydration-shell volume shell_volume197220 ų
Envelope diameter envelope_diameter257.0 Å
Shell Rg shell_rg73.31 Å
Envelope Rg envelope_rg74.83 Å
Shape Rg shape_rg76.46 Å
Total Rg total_rg76.17 Å
Total atoms total_atoms114486
Residues n_residues7618
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax215.7 Å
Rg (real space) rg_real74.88 Å
Rg uncertainty (real space) rg_real_error0.81 Å
I(0) (real space) i0_real9.4190e+09
I(0) uncertainty (real space) i0_real_error1.6190e+08
Rg (reciprocal space) rg_reciprocal75.85 Å
I(0) (reciprocal space) i0_reciprocal9563000000.0000
Solution quality estimate total_estimate0.8903
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary97.1 Å
Skewness Skewness skewness0.395
Kurtosis Kurtosis kurtosis-0.194
Angular range angular_range— – 0.1000 Å−1
Current regularization parameter α current_alpha0.1733
Highest regularization parameter α highest_alpha417100000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.920; Stabil: 0.993; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.661
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (7)

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8. Citations (1)

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9. Files and Curves (10)