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- PDB-4hxg: Pyrococcus horikoshii acylaminoacyl peptidase (orthorhombic cryst... -

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Basic information

Entry
Database: PDB / ID: 4hxg
TitlePyrococcus horikoshii acylaminoacyl peptidase (orthorhombic crystal form)
ComponentsPutative uncharacterized protein PH0594
KeywordsHYDROLASE / self-compartmentalization / beta-propeller / alpha/beta hyrdolase fold
Function / homology
Function and homology information


serine-type peptidase activity / proteolysis / metal ion binding
Similarity search - Function
WD40-like beta propeller / WD40-like Beta Propeller Repeat / Peptidase S9, prolyl oligopeptidase, catalytic domain / Prolyl oligopeptidase family / Six-bladed beta-propeller, TolB-like / Alpha/Beta hydrolase fold, catalytic domain / Alpha/Beta hydrolase fold / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
HEXANE-1,6-DIOL / Peptidase S9 prolyl oligopeptidase catalytic domain-containing protein
Similarity search - Component
Biological speciesPyrococcus horikoshii (archaea)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å
AuthorsKiss-Szeman, A. / Menyhard, D.K. / Tichy-Racs, E. / Hornung, B. / Radi, K. / Szeltner, Z. / Domokos, K. / Szamosi, I. / Naray-Szabo, G. / Polgar, L. / Harmat, V.
Citation
Journal: J.Biol.Chem. / Year: 2013
Title: A Self-compartmentalizing Hexamer Serine Protease from Pyrococcus Horikoshii: SUBSTRATE SELECTION ACHIEVED THROUGH MULTIMERIZATION.
Authors: Menyhard, D.K. / Kiss-Szeman, A. / Tichy-Racs, E. / Hornung, B. / Radi, K. / Szeltner, Z. / Domokos, K. / Szamosi, I. / Naray-Szabo, G. / Polgar, L. / Harmat, V.
#1: Journal: Biochim.Biophys.Acta / Year: 2009
Title: Characterization of a novel acylaminoacyl peptidase with hexameric structure and endopeptidase activity.
Authors: Szeltner, Z. / Kiss, A.L. / Domokos, K. / Harmat, V. / Naray-Szabo, G. / Polgar, L.
History
DepositionNov 9, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 8, 2013Provider: repository / Type: Initial release
Revision 1.1May 15, 2013Group: Database references
Revision 1.2Jul 3, 2013Group: Database references
Revision 1.3Sep 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_alt_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_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_alt_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.pdbx_dist_value / _struct_conn.pdbx_ptnr1_label_alt_id / _struct_conn.pdbx_ptnr2_label_alt_id / _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_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: Putative uncharacterized protein PH0594
B: Putative uncharacterized protein PH0594
C: Putative uncharacterized protein PH0594
D: Putative uncharacterized protein PH0594
E: Putative uncharacterized protein PH0594
F: Putative uncharacterized protein PH0594
G: Putative uncharacterized protein PH0594
H: Putative uncharacterized protein PH0594
I: Putative uncharacterized protein PH0594
J: Putative uncharacterized protein PH0594
K: Putative uncharacterized protein PH0594
L: Putative uncharacterized protein PH0594
hetero molecules


Theoretical massNumber of molelcules
Total (without water)883,49761
Polymers879,84312
Non-polymers3,65449
Water20,6631147
1
A: Putative uncharacterized protein PH0594
B: Putative uncharacterized protein PH0594
C: Putative uncharacterized protein PH0594
D: Putative uncharacterized protein PH0594
E: Putative uncharacterized protein PH0594
F: Putative uncharacterized protein PH0594
hetero molecules


Theoretical massNumber of molelcules
Total (without water)442,67241
Polymers439,9226
Non-polymers2,75035
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area34060 Å2
ΔGint-152 kcal/mol
Surface area121200 Å2
MethodPISA
2
G: Putative uncharacterized protein PH0594
H: Putative uncharacterized protein PH0594
I: Putative uncharacterized protein PH0594
J: Putative uncharacterized protein PH0594
K: Putative uncharacterized protein PH0594
L: Putative uncharacterized protein PH0594
hetero molecules


Theoretical massNumber of molelcules
Total (without water)440,82520
Polymers439,9226
Non-polymers90314
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area27630 Å2
ΔGint-162 kcal/mol
Surface area122010 Å2
MethodPISA
Unit cell
Length a, b, c (Å)183.310, 183.800, 275.740
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein
Putative uncharacterized protein PH0594


Mass: 73320.281 Da / Num. of mol.: 12 / Mutation: S466A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pyrococcus horikoshii (archaea)
Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3
Gene: PH0594 / Plasmid: pET15b / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta(DE3) / References: UniProt: O58323, acylaminoacyl-peptidase
#2: Chemical...
ChemComp-HEZ / HEXANE-1,6-DIOL


Mass: 118.174 Da / Num. of mol.: 26 / Source method: obtained synthetically / Formula: C6H14O2
#3: Chemical...
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 21 / Source method: obtained synthetically / Formula: Mg
#4: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1147 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.64 Å3/Da / Density % sol: 53.4 %

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 1.0715 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jun 29, 2006 / Details: mirrors
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0715 Å / Relative weight: 1
ReflectionResolution: 2.65→20 Å / Num. all: 255208 / Num. obs: 255208 / % possible obs: 94.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 4.39 % / Biso Wilson estimate: 50.89 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 16.47
Reflection shellResolution: 2.65→2.72 Å / Redundancy: 4.335 % / Rmerge(I) obs: 0.69 / Mean I/σ(I) obs: 2.36 / Num. unique all: 19084 / % possible all: 96.8

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Processing

Software
NameVersionClassification
MxCuBEdata collection
MOLREPphasing
PHENIX(phenix.refine: 1.7_650)refinement
XDSdata reduction
XSCALEdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4HXF
Resolution: 2.7→19.98 Å / SU ML: 0.41 / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Phase error: 24.85 / Stereochemistry target values: ML / Details: Ramachandran restraints were applied
RfactorNum. reflection% reflectionSelection details
Rfree0.2407 1751 0.79 %thin shells
Rwork0.1999 ---
all0.2002 222127 --
obs0.2002 222127 87.59 %-
Solvent computationShrinkage radii: 0.95 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 40.004 Å2 / ksol: 0.276 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--10.7705 Å2-0 Å2-0 Å2
2---8.7263 Å2-0 Å2
3----21.1662 Å2
Refinement stepCycle: LAST / Resolution: 2.7→19.98 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms58377 0 231 1147 59755
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00560324
X-RAY DIFFRACTIONf_angle_d0.97981727
X-RAY DIFFRACTIONf_dihedral_angle_d14.13621378
X-RAY DIFFRACTIONf_chiral_restr0.0778515
X-RAY DIFFRACTIONf_plane_restr0.00510492
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.7-2.77280.38451430.339314464X-RAY DIFFRACTION76
2.7728-2.85420.3787740.322715080X-RAY DIFFRACTION78
2.8542-2.9460.37241540.304315350X-RAY DIFFRACTION80
2.946-3.0510.2931860.267416076X-RAY DIFFRACTION83
3.051-3.17270.28711810.234916648X-RAY DIFFRACTION87
3.1727-3.31650.2572860.223517115X-RAY DIFFRACTION89
3.3165-3.49040.25511830.213817458X-RAY DIFFRACTION91
3.4904-3.70780.2452920.210117761X-RAY DIFFRACTION92
3.7078-3.9920.25891900.190117905X-RAY DIFFRACTION92
3.992-4.38990.1964910.158818048X-RAY DIFFRACTION93
4.3899-5.01630.16751920.136818119X-RAY DIFFRACTION93
5.0163-6.28720.2384940.175218159X-RAY DIFFRACTION93
6.2872-19.98070.20151850.171818193X-RAY DIFFRACTION91
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
10.0244-0.0257-0.05010.0140.02350.0798-0.12660.0308-0.1833-0.03050.0233-0.0180.21250.0955-0.0650.35570.01810.12070.3075-0.09590.395766.8984-13.189-32.1439
20.0397-0.00270.00350.0686-0.01290.0231-0.07370.2249-0.0493-0.2498-0.0487-0.01970.03180.0297-0.1609-0.0246-0.1030.00030.098-0.3364-0.438258.860412.4611-45.6647
30.01990.0094-0.00590.00840.0050.0283-0.08960.0814-0.1279-0.0344-0.00960.00240.171-0.1386-0.10330.4629-0.17660.09280.3373-0.13360.480820.7687-21.0762-21.0321
40.04840.0236-0.03080.02030.00370.0445-0.08720.0272-0.14350.0331-0.04840.07630.183-0.1756-0.14420.3938-0.20620.1230.3849-0.08080.42992.7328-18.07462.8106
50.0052-0.0065-0.00180.01410.01070.0186-0.0267-0.033-0.181-0.0346-0.02360.00040.26830.06290.00760.59590.12670.18920.19290.08670.562355.4937-37.19367.9718
60.0259-0.0170.03180.0132-0.01390.0315-0.0306-0.0715-0.10330.0479-0.021-0.17270.2120.1131-0.01240.53310.34360.12510.5680.2130.633380.3449-26.50421.0682
70.0334-0.0127-0.01880.0059-0.01080.0161-0.00830.00530.0060.0076-0.02250.0305-0.03510.0176-0.03660.0974-0.0271-0.0040.1655-0.00210.151156.661239.6913-7.2414
80.01750.0173-0.02080.0263-0.00590.0148-0.00240.0061-0.0172-0.03970.0009-0.0952-0.03380.11550.00080.1586-0.06460.0070.3189-0.00720.27183.027228.7535-16.9945
90.012-0.0025-0.01680.00730.00680.0649-0.0277-0.11750.00790.04080.0382-0.01450.0308-0.0670.00740.17970.0550.00320.30730.00660.283218.871824.026617.6477
100.062-0.00590.01160.00640.02120.0254-0.0395-0.00180.0345-0.0247-0.00230.0949-0.0151-0.2439-0.0870.13720.0269-0.0310.3875-0.02380.27653.730621.1601-8.381
110.02410.0335-0.01780.0148-0.02220.0437-0.0241-0.1563-0.03380.029-0.074-0.05370.00770.1777-0.08450.14830.0084-0.02840.38070.07310.215763.222615.724433.856
120.02140.01220.01830.06410.03590.0475-0.0619-0.21570.00850.175-0.18650.0080.1040.0199-0.09150.20390.1569-0.03160.27670.31530.090453.1793-9.691246.5829
130.04020.022-0.04440.06470.00360.1353-0.06250.012-0.0574-0.0706-0.06860.01540.12760.0743-0.13140.64320.04360.06160.3143-0.01240.2216121.7459-17.273134.3139
140.09810.01840.03360.0531-0.02590.1189-0.06090.0818-0.0187-0.1472-0.0739-0.0571-0.08440.1384-0.02460.58330.08930.10590.65050.07430.2914147.0101-7.207121.694
15-0.004-0.01410.00890.0509-0.05990.06990.00950.04290.03730.0881-0.01150.0023-0.18320.06310.02460.8306-0.00740.00750.24660.02680.2747113.393926.758551.5068
160.00280.00310.01620.04240.01420.02710.0138-0.06120.05570.1493-0.01520.0106-0.19530.01430.01761.2329-0.0981-0.07220.1353-0.06440.2581116.547141.35277.4116
170.01360.0126-0.00450.03970.00090.02110.0173-0.03460.00120.1165-0.03020.05780.0123-0.0357-0.00470.6758-0.01360.04570.3327-0.02110.332197.9796-11.512875.6908
180.01360.00230.00050.0367-0.02770.02290.0207-0.0541-0.04510.1105-0.00790.05030.1404-0.0270.01450.8299-0.02890.04550.2111-0.00070.2544109.0762-37.809985.3511
190.0402-0.01150.05950.0422-0.00630.1113-0.01090.08310.0345-0.00030.0047-0.15480.00620.20110.080.34350.0548-0.05960.9940.28580.4073174.2594-10.129260.2677
200.02630.00070.00690.0340.03650.03310.0570.0847-0.0519-0.0113-0.0023-0.09370.0820.14050.01470.74220.39290.11530.79670.1520.4944163.7937-34.505646.5798
210.04280.01780.02410.00370.01070.0118-0.0311-0.01060.00140.0726-0.0533-0.1225-0.18410.1266-0.02960.9141-0.4558-0.36920.71680.18250.4966158.233624.161689.6227
220.00510.0150.00590.0315-0.00650.01030.00040.02260.07770.0585-0.0369-0.0969-0.11110.08740.00931.0008-0.5836-0.27750.50980.21970.56155.412942.330266.0871
230.0382-0.0101-0.00860.0061-0.00250.0212-0.0461-0.0004-0.0123-0.0147-0.069-0.05650.12910.2016-0.07820.75060.0469-0.13620.81320.20370.4787151.0265-21.8975100.2318
240.15650.0421-0.02640.0604-0.0080.0171-0.0741-0.2502-0.01210.12-0.0743-0.0730.08740.11160.01450.6442-0.0623-0.07360.42040.03870.0768125.4053-14.0332114.0552
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resseq 4:340)
2X-RAY DIFFRACTION2chain 'A' and (resseq 350:618)
3X-RAY DIFFRACTION3chain 'B' and (resseq 4:340)
4X-RAY DIFFRACTION4chain 'B' and (resseq 350:618)
5X-RAY DIFFRACTION5chain 'C' and (resseq 4:340)
6X-RAY DIFFRACTION6chain 'C' and (resseq 350:618)
7X-RAY DIFFRACTION7chain 'D' and (resseq 4:340)
8X-RAY DIFFRACTION8chain 'D' and (resseq 350:618)
9X-RAY DIFFRACTION9chain 'E' and (resseq 4:340)
10X-RAY DIFFRACTION10chain 'E' and (resseq 350:618)
11X-RAY DIFFRACTION11chain 'F' and (resseq 4:340)
12X-RAY DIFFRACTION12chain 'F' and (resseq 350:618)
13X-RAY DIFFRACTION13chain 'G' and (resseq 4:340)
14X-RAY DIFFRACTION14chain 'G' and (resseq 350:618)
15X-RAY DIFFRACTION15chain 'H' and (resseq 4:340)
16X-RAY DIFFRACTION16chain 'H' and (resseq 350:618)
17X-RAY DIFFRACTION17chain 'I' and (resseq 4:340)
18X-RAY DIFFRACTION18chain 'I' and (resseq 350:618)
19X-RAY DIFFRACTION19chain 'J' and (resseq 4:340)
20X-RAY DIFFRACTION20chain 'J' and (resseq 350:618)
21X-RAY DIFFRACTION21chain 'K' and (resseq 4:340)
22X-RAY DIFFRACTION22chain 'K' and (resseq 350:618)
23X-RAY DIFFRACTION23chain 'L' and (resseq 4:340)
24X-RAY DIFFRACTION24chain 'L' and (resseq 350:618)

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