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9yx1

Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis

Method: ELECTRON MICROSCOPY Dmax: 213.8 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

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 × 20 PDB declaration: 20-meric（20） Consistent with protein copy count Chain F； UniProt 1–517 Chain O； UniProt 1–517 Not recorded Propionyl-CoA carboxylase beta chain × 4 （A0QTE7） Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit × 12 （A0QTE1） Acetyl-/propionyl-coenzyme A carboxylase AccE5 × 2 （A0QTE6） BTN BIOTIN × 6 BCT BICARBONATE ION × 2 ELECTRON MICROSCOPY cryo-EM buffer：pH 6 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.50 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 9YX1 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 ligand/ion Different experimental conditions 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
9TDM Cryo-EM structure of AccA3/AccD4/AccD5/AccE5 in complex with Propionyl-CoA Deposited 2025-11-24 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: 16-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 2.40 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 ligand/ion 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 ligand/ion 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 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 1
Chains and sequence ranges Author chain F； PDBConstruct 1–517； UniProt 1–517 Author chain O； 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 × 20 PDB declaration: 20-meric（20） Consistent with protein copy count Chain G； UniProt 1–542 Chain H； UniProt 1–542 Chain M； UniProt 1–542 Chain N； UniProt 1–542 Not recorded Propionyl-CoA carboxylase beta chain × 2 （A0R616） Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit × 12 （A0QTE1） Acetyl-/propionyl-coenzyme A carboxylase AccE5 × 2 （A0QTE6） BTN BIOTIN × 6 BCT BICARBONATE ION × 2 ELECTRON MICROSCOPY cryo-EM buffer：pH 6 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.50 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 9YX1 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 ligand/ion Different experimental conditions 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
9TDM Cryo-EM structure of AccA3/AccD4/AccD5/AccE5 in complex with Propionyl-CoA Deposited 2025-11-24 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: 16-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 2.40 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 ligand/ion 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 ligand/ion 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 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 2
Chains and sequence ranges Author chain G； PDBConstruct 1–542； UniProt 1–542 Author chain H； PDBConstruct 1–542； UniProt 1–542 Author chain M； PDBConstruct 1–542； UniProt 1–542 Author chain N； PDBConstruct 1–542； UniProt 1–542

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 × 20 PDB declaration: 20-meric（20） Consistent with protein copy count Chain A； UniProt 1–598 Chain B； UniProt 1–598 Chain C； UniProt 1–598 Chain D； UniProt 1–598 Chain I； UniProt 1–598 Chain J； UniProt 1–598 Chain K； UniProt 1–598 Chain L； UniProt 1–598 Chain Q； UniProt 1–598 Chain R； UniProt 1–598 Chain S； UniProt 1–598 Chain T； 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） BTN BIOTIN × 6 BCT BICARBONATE ION × 2 ELECTRON MICROSCOPY cryo-EM buffer：pH 6 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.50 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 9YX1 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 ligand/ion Different experimental conditions 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 ligand/ion Different experimental conditions 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
9TDM Cryo-EM structure of AccA3/AccD4/AccD5/AccE5 in complex with Propionyl-CoA Deposited 2025-11-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: 16-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 A3e 1–598（598 aa）
Chain A3f 1–598（598 aa）
Chain A3g 1–598（598 aa）
Chain A3h 1–598（598 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 2.40 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 ligand/ion 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 ligand/ion 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 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 3
Chains and sequence ranges Author chain A； PDBConstruct 1–598； UniProt 1–598 Author chain B； PDBConstruct 1–598； UniProt 1–598 Author chain C； PDBConstruct 1–598； UniProt 1–598 Author chain D； PDBConstruct 1–598； UniProt 1–598 Author chain I； PDBConstruct 1–598； UniProt 1–598 Author chain J； PDBConstruct 1–598； UniProt 1–598 Author chain K； PDBConstruct 1–598； UniProt 1–598 Author chain L； PDBConstruct 1–598； UniProt 1–598 Author chain Q； PDBConstruct 1–598； UniProt 1–598 Author chain R； PDBConstruct 1–598； UniProt 1–598 Author chain S； PDBConstruct 1–598； UniProt 1–598 Author chain T； PDBConstruct 1–598； UniProt 1–598

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 × 20 PDB declaration: 20-meric（20） Consistent with protein copy count Chain E； UniProt 1–94 Chain P； UniProt 1–94 Not recorded Propionyl-CoA carboxylase beta chain × 2 （A0R616） Propionyl-CoA carboxylase beta chain × 4 （A0QTE7） Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit × 12 （A0QTE1） BTN BIOTIN × 6 BCT BICARBONATE ION × 2 ELECTRON MICROSCOPY cryo-EM buffer：pH 6 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.50 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 9YX1 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 ligand/ion Different experimental conditions 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 ligand/ion Different experimental conditions 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
9TDM Cryo-EM structure of AccA3/AccD4/AccD5/AccE5 in complex with Propionyl-CoA Deposited 2025-11-24 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: 16-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 2.40 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 ligand/ion 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 ligand/ion 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 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 E； PDBConstruct 1–94； UniProt 1–94 Author chain P； 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 9yx1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9yx1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9yx1
Deposition date deposition_date2025-10-26
Structure title titleStructure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis
Keywords keywordsCarboxylase, transferase, lipid synthesis, mycolic acid synthesis, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier68.45 Å
Radius of gyration Rg (electron density) rg_electron68.09 Å
Forward intensity I(0) i06593550000.00
Molecular weight molecular_weight689660.0 kDa
Excluded volume excluded_volume864790 ų
Envelope volume envelope_volume1327000 ų
Hydration-shell volume shell_volume164290 ų
Envelope diameter envelope_diameter240.3 Å
Shell Rg shell_rg67.03 Å
Envelope Rg envelope_rg68.00 Å
Shape Rg shape_rg68.19 Å
Total Rg total_rg67.73 Å
Total atoms total_atoms48731
Residues n_residues7040
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 dmax213.8 Å
Rg (real space) rg_real68.50 Å
Rg uncertainty (real space) rg_real_error1.43 Å
I(0) (real space) i0_real6.5900e+09
I(0) uncertainty (real space) i0_real_error1.3150e+08
Rg (reciprocal space) rg_reciprocal67.98 Å
I(0) (reciprocal space) i0_reciprocal6586000000.0000
Solution quality estimate total_estimate0.8273
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary83.7 Å
Skewness Skewness skewness0.501
Kurtosis Kurtosis kurtosis0.017
Angular range angular_range— – 0.1150 Å−1
Current regularization parameter α current_alpha0.0007
Highest regularization parameter α highest_alpha445000000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.848; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.214
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

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8. Citations (1)

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9. Files and Curves (10)