6E97

Crystal structure of the aryl acid adenylating enzyme FscC from Fuscachelin NRPS in complex with DHB-adenylate

PDB DOI: https://doi.org/10.2210/pdb6E97/pdb

Classification: LIGASE
Organism(s): Thermobifida fusca YX
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2018-07-31 Released: 2019-08-21
Deposition Author(s): Bruner, S.D., Zagulyaeva, A.A.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.80 Å
R-Value Free: 0.217
R-Value Work: 0.184
R-Value Observed: 0.194

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Ligand Structure Quality Assessment

This is version 1.2 of the entry. See complete history.

Literature

Implication of MbtH-like proteins in crystallization of the independent NRPS A domains. Crystal structure of FscC: supporting rationale for revised mechanism of freestanding aryl acid adenylating enzymes

Bruner, S.D., Zagulyaeva, A.A.

To be published.

Macromolecule Content

Total Structure Weight: 120.65 kDa
Atom Count: 8,937
Modelled Residue Count: 1,072
Deposited Residue Count: 1,092
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
2,3-dihydroxybenzoate-AMP ligase	A, B	546	Thermobifida fusca YX	Mutation(s): 0 Gene Names: Tfu_1871
UniProt
Find proteins for Q47NR5 (Thermobifida fusca (strain YX)) Explore Q47NR5 Go to UniProtKB: Q47NR5
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q47NR5
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 3 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
J2J Query on J2J Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain E [auth B] MOL2 format, chain C [auth A] MOL2 format, chain E [auth B]	C [auth A], E [auth B]	5'-O-[(S)-[(2,3-dihydroxybenzene-1-carbonyl)oxy](hydroxy)phosphoryl]adenosine C₁₇ H₁₈ N₅ O₁₀ P ULPVJDOMCRTJSN-RVXWVPLUSA-N		Interactions Focus chain C [auth A] Focus chain E [auth B] Interactions & Density Focus chain C [auth A] Focus chain E [auth B]
SO4 Query on SO4 Download Ideal Coordinates CCD File SDF format, chain D [auth A] MOL2 format, chain D [auth A]	D [auth A]	SULFATE ION O₄ S QAOWNCQODCNURD-UHFFFAOYSA-L		Interactions Focus chain D [auth A] Interactions & Density Focus chain D [auth A]
GOL Query on GOL Download Ideal Coordinates CCD File SDF format, chain F [auth B] MOL2 format, chain F [auth B]	F [auth B]	GLYCEROL C₃ H₈ O₃ PEDCQBHIVMGVHV-UHFFFAOYSA-N		Interactions Focus chain F [auth B] Interactions & Density Focus chain F [auth B]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.80 Å
R-Value Free: 0.217
R-Value Work: 0.184
R-Value Observed: 0.194
Space Group: C 1 2 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 206.127	α = 90
b = 51.327	β = 119.88
c = 111.363	γ = 90

Software Package:

Software Name	Purpose
PHENIX	refinement
DENZO	data reduction
SCALEPACK	data scaling
PHASER	phasing

Structure Validation

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Entry History

Deposition Data

Released Date: 2019-08-21

Deposition Author(s):

Bruner, S.D.

Zagulyaeva, A.A.

Revision History (Full details and data files)

Version 1.0: 2019-08-21
Type: Initial release
Version 1.1: 2019-08-28
Changes: Data collection, Database references, Structure summary
Version 1.2: 2023-10-11
Changes: Data collection, Database references, Refinement description

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6E97

Crystal structure of the aryl acid adenylating enzyme FscC from Fuscachelin NRPS in complex with DHB-adenylate

Implication of MbtH-like proteins in crystallization of the independent NRPS A domains. Crystal structure of FscC: supporting rationale for revised mechanism of freestanding aryl acid adenylating enzymes

Entity ID: 1

UniProt

Entity Groups

Sequence Annotations

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Experimental Data

Structure Validation

Ligand Structure Quality Assessment

Deposition Data

Revision History (Full details and data files)