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- PDB-2glj: crystal structure of aminopeptidase I from Clostridium acetobutylicum -

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Basic information

Entry
Database: PDB / ID: 2glj
Titlecrystal structure of aminopeptidase I from Clostridium acetobutylicum
ComponentsProbable M18-family aminopeptidase 1
KeywordsHYDROLASE / aminopeptidase I / NYSGXRC / Structural Genomics / PSI / Protein Structure Initiative / New York SGX Research Center for Structural Genomics
Function / homology
Function and homology information


Hydrolases; Acting on peptide bonds (peptidases); Aminopeptidases / aminopeptidase activity / metallopeptidase activity / zinc ion binding
Similarity search - Function
M18 family aminopeptidase 1, putative / Aminopeptidase i, Domain 2 / Aminopeptidase i, Domain 2 / Peptidase M18 / Peptidase M18, domain 2 / Aminopeptidase I zinc metalloprotease (M18) / Zn peptidases / Aminopeptidase / Roll / 3-Layer(aba) Sandwich ...M18 family aminopeptidase 1, putative / Aminopeptidase i, Domain 2 / Aminopeptidase i, Domain 2 / Peptidase M18 / Peptidase M18, domain 2 / Aminopeptidase I zinc metalloprotease (M18) / Zn peptidases / Aminopeptidase / Roll / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
: / Probable M18 family aminopeptidase 1
Similarity search - Component
Biological speciesClostridium acetobutylicum (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å
AuthorsMin, T. / Shapiro, L. / Burley, S.K. / New York SGX Research Center for Structural Genomics (NYSGXRC)
CitationJournal: To be Published
Title: crystal structure of aminopeptidase I from Clostridium acetobutylicum
Authors: Min, T. / Shapiro, L.
History
DepositionApr 4, 2006Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 13, 2006Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 3, 2021Group: Database references / Derived calculations / Structure summary
Category: audit_author / pdbx_struct_conn_angle ...audit_author / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _audit_author.identifier_ORCID / _pdbx_struct_conn_angle.ptnr1_auth_comp_id ..._audit_author.identifier_ORCID / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_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.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_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.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _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_asym_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_ref_seq_dif.details / _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: Probable M18-family aminopeptidase 1
B: Probable M18-family aminopeptidase 1
C: Probable M18-family aminopeptidase 1
D: Probable M18-family aminopeptidase 1
E: Probable M18-family aminopeptidase 1
F: Probable M18-family aminopeptidase 1
G: Probable M18-family aminopeptidase 1
H: Probable M18-family aminopeptidase 1
I: Probable M18-family aminopeptidase 1
J: Probable M18-family aminopeptidase 1
K: Probable M18-family aminopeptidase 1
L: Probable M18-family aminopeptidase 1
M: Probable M18-family aminopeptidase 1
N: Probable M18-family aminopeptidase 1
O: Probable M18-family aminopeptidase 1
P: Probable M18-family aminopeptidase 1
Q: Probable M18-family aminopeptidase 1
R: Probable M18-family aminopeptidase 1
S: Probable M18-family aminopeptidase 1
T: Probable M18-family aminopeptidase 1
U: Probable M18-family aminopeptidase 1
V: Probable M18-family aminopeptidase 1
W: Probable M18-family aminopeptidase 1
X: Probable M18-family aminopeptidase 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)1,242,58672
Polymers1,239,94924
Non-polymers2,63748
Water94,2725233
1
A: Probable M18-family aminopeptidase 1
B: Probable M18-family aminopeptidase 1
C: Probable M18-family aminopeptidase 1
D: Probable M18-family aminopeptidase 1
E: Probable M18-family aminopeptidase 1
F: Probable M18-family aminopeptidase 1
G: Probable M18-family aminopeptidase 1
H: Probable M18-family aminopeptidase 1
I: Probable M18-family aminopeptidase 1
J: Probable M18-family aminopeptidase 1
K: Probable M18-family aminopeptidase 1
L: Probable M18-family aminopeptidase 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)621,29336
Polymers619,97512
Non-polymers1,31924
Water21612
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area105790 Å2
ΔGint-576 kcal/mol
Surface area176750 Å2
MethodPISA
2
M: Probable M18-family aminopeptidase 1
N: Probable M18-family aminopeptidase 1
O: Probable M18-family aminopeptidase 1
P: Probable M18-family aminopeptidase 1
Q: Probable M18-family aminopeptidase 1
R: Probable M18-family aminopeptidase 1
S: Probable M18-family aminopeptidase 1
T: Probable M18-family aminopeptidase 1
U: Probable M18-family aminopeptidase 1
V: Probable M18-family aminopeptidase 1
W: Probable M18-family aminopeptidase 1
X: Probable M18-family aminopeptidase 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)621,29336
Polymers619,97512
Non-polymers1,31924
Water21612
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area105840 Å2
ΔGint-575 kcal/mol
Surface area177090 Å2
MethodPISA
Unit cell
Length a, b, c (Å)121.708, 129.680, 222.728
Angle α, β, γ (deg.)89.88, 90.00, 116.68
Int Tables number1
Space group name H-MP1

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Components

#1: Protein ...
Probable M18-family aminopeptidase 1


Mass: 51664.551 Da / Num. of mol.: 24
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Clostridium acetobutylicum (bacteria) / Gene: apeA / Production host: Escherichia coli (E. coli)
References: UniProt: Q97K30, Hydrolases; Acting on peptide bonds (peptidases); Aminopeptidases
#2: Chemical...
ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 48 / Source method: obtained synthetically / Formula: Mn
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 5233 / Source method: isolated from a natural source / Formula: H2O

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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: 2.53 Å3/Da / Density % sol: 51.43 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop
Details: 7% EtOH, 0.05M NaCl, 0.01M MnCl2, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 0.978 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jan 1, 2005
RadiationMonochromator: SI(111)DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.978 Å / Relative weight: 1
ReflectionResolution: 2.8→20 Å / Num. obs: 311235 / % possible obs: 78.5 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1

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Processing

Software
NameVersionClassification
CNS1.1refinement
CBASSdata collection
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.2→19.95 Å / Rfactor Rfree error: 0.003 / Data cutoff high absF: 192230.62 / Data cutoff low absF: 0 / Isotropic thermal model: GROUP / Cross valid method: THROUGHOUT / σ(F): 2
RfactorNum. reflection% reflectionSelection details
Rfree0.297 10245 4.3 %RANDOM
Rwork0.25 ---
all0.25 240681 --
obs0.25 240681 60.1 %-
Solvent computationSolvent model: FLAT MODEL / Bsol: 10 Å2 / ksol: 0.180129 e/Å3
Displacement parametersBiso mean: 30.6 Å2
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å20 Å2
2--0 Å20 Å2
3---0 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.52 Å0.41 Å
Luzzati d res low-5 Å
Luzzati sigma a0.74 Å0.6 Å
Refinement stepCycle: LAST / Resolution: 3.2→19.95 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms85944 0 48 5233 91225
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.008
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_d0.79
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: 3.2→3.4 Å / Rfactor Rfree error: 0.012 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.375 1003 4.2 %
Rwork0.326 22828 -
obs--35.7 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1protein_rep.paramprotein.top
X-RAY DIFFRACTION2water_rep.paramwater.top
X-RAY DIFFRACTION3ion.paramion.top

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