[English] 日本語
Yorodumi
- PDB-6etb: Aerobic S262Y mutation of E. coli FLRD core -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6etb
TitleAerobic S262Y mutation of E. coli FLRD core
ComponentsAnaerobic nitric oxide reductase flavorubredoxin
KeywordsOXIDOREDUCTASE / Flavorubredoxin / flavodiiron protein / diiron center / nitric oxide reductase
Function / homology
Function and homology information


nitric oxide reductase activity / nitric oxide catabolic process / oxidoreductase activity, acting on other nitrogenous compounds as donors / response to nitric oxide / FMN binding / electron transfer activity / iron ion binding / protein-containing complex / identical protein binding / cytoplasm
Similarity search - Function
Anaerobic nitric oxide reductase flavorubredoxin / Rubredoxin-oxygen oxidoreductase / ODP domain / ODP family beta lactamase / Rubredoxin domain / Rubredoxin / Rubredoxin-like domain / Rubredoxin-like domain profile. / Flavodoxin domain / Metallo-beta-lactamase superfamily ...Anaerobic nitric oxide reductase flavorubredoxin / Rubredoxin-oxygen oxidoreductase / ODP domain / ODP family beta lactamase / Rubredoxin domain / Rubredoxin / Rubredoxin-like domain / Rubredoxin-like domain profile. / Flavodoxin domain / Metallo-beta-lactamase superfamily / Ribonuclease Z/Hydroxyacylglutathione hydrolase-like / Metallo-beta-lactamase; Chain A / Metallo-beta-lactamase superfamily / Metallo-beta-lactamase / Flavodoxin / Flavodoxin-like domain profile. / Flavodoxin/nitric oxide synthase / Ribonuclease Z/Hydroxyacylglutathione hydrolase-like / Flavoprotein-like superfamily / 4-Layer Sandwich / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
: / FLAVIN MONONUCLEOTIDE / OXYGEN ATOM / OXYGEN MOLECULE / Anaerobic nitric oxide reductase flavorubredoxin
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.905 Å
AuthorsBorges, P.T. / Romao, C.V. / Carrondo, M.A. / Teixeira, M. / Frazao, C.
CitationJournal: To Be Published
Title: A tyrosine mutation in E. coli flavodiiron protein increases radiation sensitivity in the crystal structure
Authors: Borges, P.T. / Romao, C.V. / Carrondo, M.A. / Teixeira, M. / Frazao, C.
History
DepositionOct 26, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 7, 2018Provider: repository / Type: Initial release
Revision 1.1Jan 17, 2024Group: 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 / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_dist_value / _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

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Anaerobic nitric oxide reductase flavorubredoxin
B: Anaerobic nitric oxide reductase flavorubredoxin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)95,44012
Polymers94,2082
Non-polymers1,23210
Water14,088782
1
A: Anaerobic nitric oxide reductase flavorubredoxin
B: Anaerobic nitric oxide reductase flavorubredoxin
hetero molecules

A: Anaerobic nitric oxide reductase flavorubredoxin
B: Anaerobic nitric oxide reductase flavorubredoxin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)190,88024
Polymers188,4164
Non-polymers2,46420
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,y,-z1
Unit cell
Length a, b, c (Å)89.383, 64.407, 147.254
Angle α, β, γ (deg.)90.00, 91.09, 90.00
Int Tables number5
Space group name H-MI121
Components on special symmetry positions
IDModelComponents
11A-630-

HOH

-
Components

-
Protein , 1 types, 2 molecules AB

#1: Protein Anaerobic nitric oxide reductase flavorubredoxin / FlavoRb


Mass: 47104.074 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (strain K12) (bacteria)
Strain: K12 / Gene: norV, flrD, ygaI, ygaJ, ygaK, b2710, JW2680 / Production host: Escherichia coli (E. coli) / References: UniProt: Q46877

-
Non-polymers , 5 types, 792 molecules

#2: Chemical ChemComp-FMN / FLAVIN MONONUCLEOTIDE / RIBOFLAVIN MONOPHOSPHATE


Mass: 456.344 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C17H21N4O9P
#3: Chemical
ChemComp-FE / FE (III) ION


Mass: 55.845 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Fe
#4: Chemical ChemComp-OXY / OXYGEN MOLECULE


Mass: 31.999 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: O2
#5: Chemical ChemComp-O / OXYGEN ATOM


Mass: 15.999 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: O
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 782 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.28 Å3/Da / Density % sol: 45.9 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, hanging drop / pH: 5.6
Details: 1.0 UL OF PROTEIN AT 15 MG/ML WITH 2.0 UL OF CRYSTALLIZATION SOLUTION (0.1 M SODIUM CITRATE PH 5.6, 20% (W/V) PEG 4000 AND 20% (V/V) 2-PROPANOL)

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 11, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.9→75.83 Å / Num. obs: 57099 / % possible obs: 80.69 % / Redundancy: 2.3 % / Rmerge(I) obs: 0.113 / Rpim(I) all: 0.075 / Rrim(I) all: 0.137 / Net I/σ(I): 5.2
Reflection shellHighest resolution: 1.9 Å / Rpim(I) all: 0.431 / Rrim(I) all: 0.863 / % possible all: 88.7

-
Processing

Software
NameVersionClassification
PHENIXdev_1436refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4D02
Resolution: 1.905→75.758 Å / SU ML: 0.19 / Cross valid method: FREE R-VALUE / σ(F): 16.64 / Phase error: 19.98
Details: The refinement of S262Y mutation from E. coli FLRD core converged to Rwork and Rfree of 0.2174 and 0.2348, respectively, using a Rfree test set size of 1.51% (799 reflections). The final ...Details: The refinement of S262Y mutation from E. coli FLRD core converged to Rwork and Rfree of 0.2174 and 0.2348, respectively, using a Rfree test set size of 1.51% (799 reflections). The final model then was refined versus the full data, resulting a final R value of 0.1998.
RfactorNum. reflection% reflection
Rfree0.1998 799 1.51 %
Rwork0.1998 --
obs0.1998 52943 80.69 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 1.905→75.758 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6440 0 72 782 7294
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0186725
X-RAY DIFFRACTIONf_angle_d0.569123
X-RAY DIFFRACTIONf_dihedral_angle_d10.1462433
X-RAY DIFFRACTIONf_chiral_restr0.022990
X-RAY DIFFRACTIONf_plane_restr0.0021182
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.9052-1.92690.30389510.3038951X-RAY DIFFRACTION44
1.9269-1.94960.297113100.29711310X-RAY DIFFRACTION60
1.9496-1.97330.295914330.29591433X-RAY DIFFRACTION65
1.9733-1.99830.295614650.29561465X-RAY DIFFRACTION68
1.9983-2.02460.290915460.29091546X-RAY DIFFRACTION71
2.0246-2.05240.275815490.27581549X-RAY DIFFRACTION73
2.0524-2.08170.265516700.26551670X-RAY DIFFRACTION75
2.0817-2.11280.258216640.25821664X-RAY DIFFRACTION77
2.1128-2.14580.236917200.23691720X-RAY DIFFRACTION79
2.1458-2.1810.239616820.23961682X-RAY DIFFRACTION78
2.181-2.21860.239617080.23961708X-RAY DIFFRACTION78
2.2186-2.25890.234916560.23491656X-RAY DIFFRACTION77
2.2589-2.30240.231519270.23151927X-RAY DIFFRACTION87
2.3024-2.34940.227819030.22781903X-RAY DIFFRACTION88
2.3494-2.40050.227619500.22761950X-RAY DIFFRACTION90
2.4005-2.45630.22919560.2291956X-RAY DIFFRACTION90
2.4563-2.51770.216719260.21671926X-RAY DIFFRACTION89
2.5177-2.58580.216619580.21661958X-RAY DIFFRACTION89
2.5858-2.66190.216118830.21611883X-RAY DIFFRACTION87
2.6619-2.74780.208217820.20821782X-RAY DIFFRACTION81
2.7478-2.8460.208519850.20851985X-RAY DIFFRACTION91
2.846-2.960.206319830.20631983X-RAY DIFFRACTION91
2.96-3.09470.202119980.20211998X-RAY DIFFRACTION90
3.0947-3.25790.185319500.18531950X-RAY DIFFRACTION89
3.2579-3.4620.171518790.17151879X-RAY DIFFRACTION86
3.462-3.72930.168818580.16881858X-RAY DIFFRACTION84
3.7293-4.10450.156919470.15691947X-RAY DIFFRACTION89
4.1045-4.69840.144619350.14461935X-RAY DIFFRACTION87
4.6984-5.91910.159718490.15971849X-RAY DIFFRACTION83
5.9191-75.81790.161619200.16161920X-RAY DIFFRACTION84
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)
1-0.0006-0.0179-0.00060.3699-0.11270.03750.07150.02540.0424-0.1104-0.002-0.08070.05980.0569-00.1960.0216-0.05040.147-0.00760.1986-28.7562-36.6483-9.7889
20.00990.014-0.04470.0279-0.09840.29090.4089-0.0512-0.1001-0.5820.36540.1737-0.0021-0.04090.01410.32130.0150.00080.1587-0.02220.4093-10.9933-25.8163-4.6271
30.04370.12780.06080.25890.0540.22220.0785-0.0024-0.1921-0.1629-0.01190.00210.1454-0.0268-0.00290.15360.0132-0.02940.1311-0.01890.2077-29.9656-31.1157-14.0031
40.25660.0132-0.28280.05540.16161.16170.1248-0.042-0.2325-0.44860.187-0.1440.5530.46240.01240.39560.0397-0.07090.1957-0.04320.3042-25.23-37.6893-21.763
50.2287-0.0421-0.24260.2096-0.00010.20010.22670.0432-0.20440.04880.0223-0.15990.27590.14890.00010.17460.02710.01820.16960.00720.2626-26.655-26.4811-20.9155
60.12360.2225-0.33850.2796-0.09050.7436-0.13970.14020.0582-0.04870.0106-0.02890.05060.1457-0.01740.22090.0394-0.01550.20030.02420.1539-27.5933-19.2237-25.0901
70.53070.4441-0.16250.4230.08680.2640.0768-0.0099-0.08810.0375-0.02560.0167-0.00170.04410.07930.0906-0.0007-00.08850.03360.1237-32.2493-25.226-7.1384
80.0599-0.0181-0.05770.0422-0.00660.0420.0726-0.0572-0.0780.027-0.06430.0530.04390.1788-0.00030.0837-0.00090.0190.22140.02910.1444-21.8571-26.46064.6456
90.4174-0.32710.17060.2058-0.01350.54850.0141-0.0154-0.02510.2692-0.0453-0.018-0.0375-0.1281-0.00220.15540.02490.00590.16090.01730.1502-32.2496-19.4622-1.3216
100.0502-0.04040.08160.11030.01530.06630.0798-0.16990.1444-0.1612-0.1977-0.0363-0.2428-0.4312-0.00390.12180.06880.0370.23360.02920.2304-26.4152-15.89178.7624
110.3343-0.00630.30080.4662-0.06470.32890.048-0.3584-0.4242-0.01230.0085-0.0070.1177-0.01260.01760.1301-0.0044-0.00390.23170.05510.1607-4.5946-19.619719.5008
120.142-0.2019-0.01130.33040.12460.47820.0076-0.2626-0.0679-0.12570.044-0.0439-0.05950.01250.21680.07510.00920.05830.15540.0070.1356-4.1939-17.45218.4502
130.1266-0.1025-0.07170.05980.00690.11660.05070.03440.107-0.00290.1074-0.0563-0.0704-0.20330.0520.17720.01860.0010.13910.04330.15-12.7959-9.78966.0018
140.08420.01930.10060.17940.12940.156-0.1452-0.15940.1642-0.0233-0.0429-0.076-0.113-0.0579-0.04760.16810.0054-0.0170.10880.00870.1631.7491-7.840713.5113
150.17060.1459-0.02640.134-0.00350.0497-0.1585-0.59390.28290.06570.1383-0.1375-0.3938-0.0124-0.03810.1773-0.00010.01960.3636-0.05020.1059-2.8076-12.559827.0024
160.0208-0.10040.05150.2776-0.04220.0238-0.0969-0.04860.00220.0212-0.0287-0.0424-0.42010.0454-00.23850.0018-0.01350.12820.02230.1986-5.5028-30.799429.944
170.04830.0079-0.0015-0.00070.0180.0367-0.4511-0.0246-0.54050.19760.0278-0.5643-0.1435-0.55520.0020.32530.06490.07010.2162-0.04570.3054-1.2712-41.586411.8661
180.1397-0.18190.16720.4688-0.06830.10890.0242-0.05330.09490.02370.0396-0.0514-0.231-0.22350.00010.2284-0.01590.03560.17590.00930.1436-2.3451-36.356633.0067
191.98280.39510.50860.3850.5380.7858-0.05510.50040.48060.1990.2845-0.3585-0.70130.31760.02740.4819-0.116-0.16940.10730.04170.3956.7258-29.7432.6766
200.2726-0.1226-0.18510.3764-0.0480.1135-0.27260.10660.2622-0.1275-0.04470.1319-0.5257-0.0135-0.01310.2984-0.0505-0.03980.19740.02230.15965.2372-41.016533.4488
210.8853-0.47140.360.56720.44720.7706-0.1118-0.0063-0.09950.04110.2244-0.0950.0680.17970.20730.21910.0224-0.02220.15520.0470.15088.4226-48.277336.2748
220.5137-0.1101-0.23710.27710.38940.37380.06530.0419-0.02450.07610.02420.0442-0.0398-0.18320.10390.16740.0290.01790.17540.04760.1323-9.5746-42.135331.5778
230.04440.0086-0.03930.0382-0.00760.01940.0570.0444-0.1224-0.1088-0.1847-0.0391-0.361-0.0059-00.25390.0144-0.02170.21190.00680.1315-14.7455-40.88716.8183
240.1806-0.1709-0.24690.82240.40671.74160.07640.0879-0.0764-0.242-0.42330.2483-0.1118-1.0718-0.71560.0716-0.08460.0203-0.01540.2074-0.0698-14.716-47.843428.8274
250.0738-0.1110.07730.1089-0.08940.13430.1102-0.1597-0.03420.0933-0.2502-0.33790.1942-0.4221-0.01860.2211-0.04640.02120.31140.08850.2021-20.6247-51.424218.7857
260.1837-0.24110.21630.70920.1831.07240.39270.25410.22570.02050.0878-0.2142-0.5054-0.76490.51860.17560.0393-0.00660.31580.0520.0728-19.2796-47.7591-5.5333
270.4417-0.09060.26210.2241-0.32930.4783-0.07790.1098-0.0380.09480.091-0.14060.0143-0.30440.0280.1722-0.0088-0.00110.1220.0250.1798-9.4217-49.9389-0.4406
280.7382-0.1205-1.11890.43080.12381.6577-0.61270.2252-0.13110.0352-0.1128-0.13080.3542-0.4327-0.59020.10850.105-0.0917-0.03980.18280.2239-11.5062-57.60738.2497
290.06030.15490.06160.14840.01750.4236-0.0038-0.0013-0.0234-0.0438-0.0314-0.16050.3135-0.2238-0.02280.1408-0.00280.00350.11210.01980.1651-10.9526-59.5709-8.0715
300.2039-0.0036-0.10190.19030.27320.28290.09060.167-0.1815-0.11040.12160.10530.0314-0.66540.0330.1877-0.08070.02970.39270.01070.2499-24.9122-54.841-10.7066
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain A and resid 2:20)
2X-RAY DIFFRACTION2(chain A and resid 21:28)
3X-RAY DIFFRACTION3(chain A and resid 29:52)
4X-RAY DIFFRACTION4(chain A and resid 53:69)
5X-RAY DIFFRACTION5(chain A and resid 70:91)
6X-RAY DIFFRACTION6(chain A and resid 92:131)
7X-RAY DIFFRACTION7(chain A and resid 132:186)
8X-RAY DIFFRACTION8(chain A and resid 187:194)
9X-RAY DIFFRACTION9(chain A and resid 195:239)
10X-RAY DIFFRACTION10(chain A and resid 240:251)
11X-RAY DIFFRACTION11(chain A and resid 252:291)
12X-RAY DIFFRACTION12(chain A and resid 292:327)
13X-RAY DIFFRACTION13(chain A and resid 328:340)
14X-RAY DIFFRACTION14(chain A and resid 341:375)
15X-RAY DIFFRACTION15(chain A and resid 376:400)
16X-RAY DIFFRACTION16(chain B and resid 2:20)
17X-RAY DIFFRACTION17(chain B and resid 21:28)
18X-RAY DIFFRACTION18(chain B and resid 29:52)
19X-RAY DIFFRACTION19(chain B and resid 53:69)
20X-RAY DIFFRACTION20(chain B and resid 70:91)
21X-RAY DIFFRACTION21(chain B and resid 92:131)
22X-RAY DIFFRACTION22(chain B and resid 132:186)
23X-RAY DIFFRACTION23(chain B and resid 187:194)
24X-RAY DIFFRACTION24(chain B and resid 195:239)
25X-RAY DIFFRACTION25(chain B and resid 240:251)
26X-RAY DIFFRACTION26(chain B and resid 252:291)
27X-RAY DIFFRACTION27(chain B and resid 292:327)
28X-RAY DIFFRACTION28(chain B and resid 328:340)
29X-RAY DIFFRACTION29(chain B and resid 341:375)
30X-RAY DIFFRACTION30(chain B and resid 376:400)

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbjlvh1.pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more