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- PDB-1e5i: DELTA-R306 DEACETOXYCEPHALOSPORIN C SYNTHASE COMPLEXED WITH IRON ... -

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Basic information

Entry
Database: PDB / ID: 1e5i
TitleDELTA-R306 DEACETOXYCEPHALOSPORIN C SYNTHASE COMPLEXED WITH IRON AND 2-OXOGLUTARATE.
ComponentsDEACETOXYCEPHALOSPORIN C SYNTHASE
KeywordsOXIDOREDUCTASE / FERROUS OXYGENASE / CEPHALOSPORIN / 2-OXOGLUTARATE / C-TERMINUS ANTIBIOTICS / OXIDATIVE COUPLING CONTROL
Function / homology
Function and homology information


deacetoxycephalosporin-C synthase / deacetoxycephalosporin-C synthase activity / L-ascorbic acid binding / antibiotic biosynthetic process / iron ion binding
Similarity search - Function
: / Isopenicillin N synthase, conserved site / Isopenicillin N synthase signature 2. / B-lactam Antibiotic, Isopenicillin N Synthase; Chain / non-haem dioxygenase in morphine synthesis N-terminal / Isopenicillin N synthase-like, Fe(2+) 2OG dioxygenase domain / 2OG-Fe(II) oxygenase superfamily / Isopenicillin N synthase-like superfamily / Oxoglutarate/iron-dependent dioxygenase / Fe(2+) 2-oxoglutarate dioxygenase domain profile. ...: / Isopenicillin N synthase, conserved site / Isopenicillin N synthase signature 2. / B-lactam Antibiotic, Isopenicillin N Synthase; Chain / non-haem dioxygenase in morphine synthesis N-terminal / Isopenicillin N synthase-like, Fe(2+) 2OG dioxygenase domain / 2OG-Fe(II) oxygenase superfamily / Isopenicillin N synthase-like superfamily / Oxoglutarate/iron-dependent dioxygenase / Fe(2+) 2-oxoglutarate dioxygenase domain profile. / Jelly Rolls / Sandwich / Mainly Beta
Similarity search - Domain/homology
2-OXOGLUTARIC ACID / : / Deacetoxycephalosporin C synthase
Similarity search - Component
Biological speciesSTREPTOMYCES CLAVULIGERUS (bacteria)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.1 Å
AuthorsLee, H.J. / Lloyd, M.D. / Harlos, K. / Clifton, I.J. / Baldwin, J.E. / Schofield, C.J.
Citation
Journal: J.Mol.Biol. / Year: 2001
Title: Kinetic and Crystallographic Studies on Deacetoxycephalosporin C Synthase (Daocs)
Authors: Lee, H.J. / Lloyd, M.D. / Harlos, K. / Clifton, I.J. / Baldwin, J.E. / Schofield, C.J.
#1: Journal: J.Mol.Biol. / Year: 1999
Title: Studies on the Active Site of Deacetoxycephalosporin C Synthase (Daocs)
Authors: Lloyd, M.D. / Lee, H.J. / Harlos, K. / Zhang, Z.-H. / Baldwin, J.E. / Schofield, C.J. / Charnock, J.M. / Garner, C.D. / Hara, T. / Terrwisscha Van Scheltinga, A.C. / Valegard, K. / Viklund, ...Authors: Lloyd, M.D. / Lee, H.J. / Harlos, K. / Zhang, Z.-H. / Baldwin, J.E. / Schofield, C.J. / Charnock, J.M. / Garner, C.D. / Hara, T. / Terrwisscha Van Scheltinga, A.C. / Valegard, K. / Viklund, J.A.C. / Hajdu, J. / Andersson, I. / Danielsson, A. / Bhikhabhai, R.
History
DepositionJul 26, 2000Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 26, 2001Provider: repository / Type: Initial release
Revision 1.1Aug 24, 2011Group: Atomic model / Derived calculations ...Atomic model / Derived calculations / Non-polymer description / Other / Refinement description / Source and taxonomy / Structure summary / Version format compliance
Revision 1.2Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: DEACETOXYCEPHALOSPORIN C SYNTHASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,2483
Polymers34,0461
Non-polymers2022
Water2,216123
1
A: DEACETOXYCEPHALOSPORIN C SYNTHASE
hetero molecules

A: DEACETOXYCEPHALOSPORIN C SYNTHASE
hetero molecules

A: DEACETOXYCEPHALOSPORIN C SYNTHASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)102,7449
Polymers102,1383
Non-polymers6066
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-y,x-y,z1
crystal symmetry operation3_555-x+y,-x,z1
Buried area7330 Å2
ΔGint-57.9 kcal/mol
Surface area29400 Å2
MethodPISA
2


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)105.787, 105.787, 71.222
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number146
Space group name H-MH3

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Components

#1: Protein DEACETOXYCEPHALOSPORIN C SYNTHASE / RING EXPANDING ENZYME / RING EXPANDASE / DAOCS / EXPANDASE


Mass: 34046.004 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-306
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) STREPTOMYCES CLAVULIGERUS (bacteria) / Description: RECOMBINANT E.COLI / Gene: CEFE / Plasmid: PET 24A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: P18548, deacetoxycephalosporin-C synthase
#2: Chemical ChemComp-FE2 / FE (II) ION


Mass: 55.845 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Fe
#3: Chemical ChemComp-AKG / 2-OXOGLUTARIC ACID


Mass: 146.098 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C5H6O5
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 123 / Source method: isolated from a natural source / Formula: H2O
Compound detailsTHE C-TERMINAL RESIDUES THR, SER, LYS, ALA ARE DELETED. FUNCTION: DAOCS CATALYZES THE STEP FROM ...THE C-TERMINAL RESIDUES THR, SER, LYS, ALA ARE DELETED. FUNCTION: DAOCS CATALYZES THE STEP FROM PENICILLIN N TO DEACETOXY- CEPHALOSPORIN C. COFACTOR: IRON AND ASCORBATE. PATHWAY: BIOSYNTHESIS OF CEPHALOSPORIN ANTIBIOTICS. SIMILARITY: BELONGS TO THE IRONULLSCORBATE-DEPENDENT FAMILY OF OXIDOREDUCTASES. STRONG, TO CEFF.
Sequence detailsILE A 50, WRONGLY REPORTED IN DATABASE

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.42 Å3/Da / Density % sol: 48.78 %
Crystal growpH: 7
Details: 100 MM HEPES-NAOH, PH 7.0, 0.5 MM PB(OAC)2(OH2)2, 5 MM 2-OXOGLUTARATE, GLYCEROL 5-10% (W/V), 1.4-1.65 M AMMONIUM SULPHATE

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418
DetectorType: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Mar 26, 1999 / Details: YALE MIRRORS
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2.1→30 Å / Num. obs: 17034 / % possible obs: 99.9 % / Redundancy: 3.2 % / Biso Wilson estimate: 21.6 Å2 / Rmerge(I) obs: 0.108 / Rsym value: 0.118 / Net I/σ(I): 3.98
Reflection shellResolution: 2→2.11 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.423 / Mean I/σ(I) obs: 6.29 / Rsym value: 0.561 / % possible all: 100

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Processing

Software
NameVersionClassification
CNS0.9refinement
MOSFLMdata reduction
SCALAdata scaling
CNSRIGID BODY REFINEMENTphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1RXF

1rxf


Resolution: 2.1→19.99 Å / Rfactor Rfree error: 0.009 / Data cutoff high absF: 2222669.75 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
Details: DATA DETWINNED USING CCP4 PROGRAMME DETWIN (A. LESLIE)
RfactorNum. reflection% reflectionSelection details
Rfree0.242 709 4.1 %RANDOM
Rwork0.227 ---
obs0.227 17139 98.8 %-
Solvent computationSolvent model: FLAT MODEL / Bsol: 53.8284 Å2 / ksol: 0.38674 e/Å3
Displacement parametersBiso mean: 32.8 Å2
Baniso -1Baniso -2Baniso -3
1--1.1 Å21.22 Å20 Å2
2---1.1 Å20 Å2
3---2.2 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.29 Å0.26 Å
Luzzati d res low-5 Å
Luzzati sigma a0.21 Å0.2 Å
Refinement stepCycle: LAST / Resolution: 2.1→19.99 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2077 0 11 123 2211
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.012
X-RAY DIFFRACTIONc_bond_d_na
X-RAY DIFFRACTIONc_bond_d_prot
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_d_na
X-RAY DIFFRACTIONc_angle_d_prot
X-RAY DIFFRACTIONc_angle_deg1.3
X-RAY DIFFRACTIONc_angle_deg_na
X-RAY DIFFRACTIONc_angle_deg_prot
X-RAY DIFFRACTIONc_dihedral_angle_d23.1
X-RAY DIFFRACTIONc_dihedral_angle_d_na
X-RAY DIFFRACTIONc_dihedral_angle_d_prot
X-RAY DIFFRACTIONc_improper_angle_d0.72
X-RAY DIFFRACTIONc_improper_angle_d_na
X-RAY DIFFRACTIONc_improper_angle_d_prot
X-RAY DIFFRACTIONc_mcbond_it
X-RAY DIFFRACTIONc_mcangle_it
X-RAY DIFFRACTIONc_scbond_it
X-RAY DIFFRACTIONc_scangle_it
LS refinement shellResolution: 2.1→2.23 Å / Rfactor Rfree error: 0.024 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.278 137 4.7 %
Rwork0.259 2755 -
obs--100 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PROTEIN_REP.PARAMPROTEIN.TOP
X-RAY DIFFRACTION2ION.PARAMION.TOP
X-RAY DIFFRACTION3WATER_REP.PARAMWATER.TOP
X-RAY DIFFRACTION42-OXOGLUTARATE.PAR2-OXOGLUTARATE.TOP

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