8UZ2

E. coli acetyl-CoA carboxylase, narrow helical local reconstruction, 3.18 Angstrom

PDB DOI: https://doi.org/10.2210/pdb8UZ2/pdb
EM Map EMD-42831: EMDB EMDataResource

Classification: BIOSYNTHETIC PROTEIN
Organism(s): Escherichia coli
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2023-11-14 Released: 2024-11-20
Deposition Author(s): Xu, X., Silva de Sousa, A., Boram, T.J., Jiang, W., Lohman, R.J.
Funding Organization(s): National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)

Experimental Data Snapshot

Method: ELECTRON MICROSCOPY
Resolution: 3.18 Å
Aggregation State: HELICAL ARRAY
Reconstruction Method: HELICAL

wwPDB Validation 3D Report Full Report

This is version 1.0 of the entry. See complete history.

Literature

E. coli acetyl-CoA carboxylase, narrow helical local reconstruction, 3.18 Angstrom

Xu, X., Silva de Sousa, A., Boram, T.J., Jiang, W., Lohman, R.J.

To be published.

Macromolecule Content

Total Structure Weight: 281.5 kDa
Atom Count: 17,474
Modelled Residue Count: 2,246
Deposited Residue Count: 2,530
Unique protein chains: 4

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha	A, E	316	Escherichia coli	Mutation(s): 0 Gene Names: accA, b0185, JW0180 EC: 2.1.3.15
UniProt
Find proteins for P0ABD5 (Escherichia coli (strain K12)) Explore P0ABD5 Go to UniProtKB: P0ABD5
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P0ABD5
Sequence Annotations Expand
Reference Sequence

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(by identity cutoff) | 3D Structure

Entity ID: 2
Molecule	Chains	Sequence Length	Organism	Details	Image
Biotin carboxyl carrier protein of acetyl-CoA carboxylase	B, F	77	Escherichia coli	Mutation(s): 0 Gene Names: accB, fabE, b3255, JW3223
UniProt
Find proteins for P0ABD8 (Escherichia coli (strain K12)) Explore P0ABD8 Go to UniProtKB: P0ABD8
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P0ABD8
Sequence Annotations Expand
Reference Sequence

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(by identity cutoff) | 3D Structure

Entity ID: 3
Molecule	Chains	Sequence Length	Organism	Details	Image
Biotin carboxylase	C, G	446	Escherichia coli	Mutation(s): 0 Gene Names: accC, fabG, b3256, JW3224 EC: 6.3.4.14
UniProt
Find proteins for P24182 (Escherichia coli (strain K12)) Explore P24182 Go to UniProtKB: P24182
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P24182
Sequence Annotations Expand
Reference Sequence

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(by identity cutoff) | 3D Structure

Entity ID: 4
Molecule	Chains	Sequence Length	Organism	Details	Image
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta	D, H, I	284	Escherichia coli	Mutation(s): 0 Gene Names: accD, dedB, usg, b2316, JW2313 EC: 2.1.3.15
UniProt
Find proteins for P0A9Q5 (Escherichia coli (strain K12)) Explore P0A9Q5 Go to UniProtKB: P0A9Q5
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P0A9Q5
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 5 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
ACO Query on ACO Download Ideal Coordinates CCD File SDF format, chain N [auth D] SDF format, chain S [auth H] MOL2 format, chain N [auth D] MOL2 format, chain S [auth H] mmCIF format, chain N [auth D] mmCIF format, chain S [auth H]	N [auth D], S [auth H]	*ACETYL COENZYME A** C₂₃ H₃₈ N₇ O₁₇ P₃ S ZSLZBFCDCINBPY-ZSJPKINUSA-N		Interactions Focus chain N [auth D] Focus chain S [auth H] Interactions & Density Focus chain N [auth D] Focus chain S [auth H]
ADP Query on ADP Download Ideal Coordinates CCD File SDF format, chain K [auth C] SDF format, chain P [auth G] MOL2 format, chain K [auth C] MOL2 format, chain P [auth G] mmCIF format, chain K [auth C] mmCIF format, chain P [auth G]	K [auth C], P [auth G]	ADENOSINE-5'-DIPHOSPHATE C₁₀ H₁₅ N₅ O₁₀ P₂ XTWYTFMLZFPYCI-KQYNXXCUSA-N		Interactions Focus chain K [auth C] Focus chain P [auth G] Interactions & Density Focus chain K [auth C] Focus chain P [auth G]
BTN Query on BTN Download Ideal Coordinates CCD File SDF format, chain J [auth B] SDF format, chain O [auth F] MOL2 format, chain J [auth B] MOL2 format, chain O [auth F] mmCIF format, chain J [auth B] mmCIF format, chain O [auth F]	J [auth B], O [auth F]	BIOTIN C₁₀ H₁₆ N₂ O₃ S YBJHBAHKTGYVGT-ZKWXMUAHSA-N		Interactions Focus chain J [auth B] Focus chain O [auth F] Interactions & Density Focus chain J [auth B] Focus chain O [auth F]
ZN Query on ZN Download Ideal Coordinates CCD File SDF format, chain M [auth D] SDF format, chain R [auth H] MOL2 format, chain M [auth D] MOL2 format, chain R [auth H] mmCIF format, chain M [auth D] mmCIF format, chain R [auth H]	M [auth D], R [auth H]	ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N		Interactions Focus chain M [auth D] Focus chain R [auth H] Interactions & Density Focus chain M [auth D] Focus chain R [auth H]
MG Query on MG Download Ideal Coordinates CCD File SDF format, chain L [auth C] SDF format, chain Q [auth G] MOL2 format, chain L [auth C] MOL2 format, chain Q [auth G] mmCIF format, chain L [auth C] mmCIF format, chain Q [auth G]	L [auth C], Q [auth G]	MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N		Interactions Focus chain L [auth C] Focus chain Q [auth G] Interactions & Density Focus chain L [auth C] Focus chain Q [auth G]