[English] 日本語
Yorodumi
- PDB-5e1g: Crystal structure of Mycobacterium tuberculosis L,D-transpeptidas... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5e1g
TitleCrystal structure of Mycobacterium tuberculosis L,D-transpeptidase 2 with carbapenem drug T208
ComponentsL,D-transpeptidase 2
KeywordsTRANSFERASE / Peptidoglycan synthesis enzyme / cell wall enzyme
Function / homology
Function and homology information


peptidoglycan-protein cross-linking / peptidoglycan L,D-transpeptidase activity / Transferases; Acyltransferases; Aminoacyltransferases / acyltransferase activity / cell wall organization / regulation of cell shape / metal ion binding / plasma membrane
Similarity search - Function
Immunoglobulin-like - #3710 / Bacterial Ig domain, transpeptidase-associated / Bacterial Ig domain / L,D-transpeptidase catalytic domain-like / L,D-transpeptidase catalytic domain-like / : / L,D-transpeptidase (L,D-TPase) catalytic domain profile. / L,D-transpeptidase catalytic domain / L,D-transpeptidase catalytic domain-like / L,D-transpeptidase catalytic domain ...Immunoglobulin-like - #3710 / Bacterial Ig domain, transpeptidase-associated / Bacterial Ig domain / L,D-transpeptidase catalytic domain-like / L,D-transpeptidase catalytic domain-like / : / L,D-transpeptidase (L,D-TPase) catalytic domain profile. / L,D-transpeptidase catalytic domain / L,D-transpeptidase catalytic domain-like / L,D-transpeptidase catalytic domain / Prokaryotic membrane lipoprotein lipid attachment site profile. / Beta Barrel / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Chem-T8G / L,D-transpeptidase 2
Similarity search - Component
Biological speciesMycobacterium tuberculosis (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.852 Å
AuthorsKumar, P. / Lamichhane, G. / Ginell, S.L.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/Office of the Director1DP2OD008459-01 United States
CitationJournal: Nat. Chem. Biol. / Year: 2017
Title: Non-classical transpeptidases yield insight into new antibacterials.
Authors: Kumar, P. / Kaushik, A. / Lloyd, E.P. / Li, S.G. / Mattoo, R. / Ammerman, N.C. / Bell, D.T. / Perryman, A.L. / Zandi, T.A. / Ekins, S. / Ginell, S.L. / Townsend, C.A. / Freundlich, J.S. / Lamichhane, G.
History
DepositionSep 29, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 12, 2016Provider: repository / Type: Initial release
Revision 1.1Nov 9, 2016Group: Database references
Revision 1.2Nov 23, 2016Group: Database references
Revision 1.3Dec 28, 2016Group: Database references
Revision 1.4Sep 20, 2017Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.5Sep 27, 2023Group: Advisory / Data collection ...Advisory / Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_unobs_or_zero_occ_atoms
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: L,D-transpeptidase 2
B: L,D-transpeptidase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)79,4493
Polymers79,0642
Non-polymers3851
Water7,152397
1
A: L,D-transpeptidase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,9172
Polymers39,5321
Non-polymers3851
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: L,D-transpeptidase 2


Theoretical massNumber of molelcules
Total (without water)39,5321
Polymers39,5321
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
A: L,D-transpeptidase 2
hetero molecules

B: L,D-transpeptidase 2


Theoretical massNumber of molelcules
Total (without water)79,4493
Polymers79,0642
Non-polymers3851
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_548-x,y-1/2,-z+31
Buried area1920 Å2
ΔGint-13 kcal/mol
Surface area30640 Å2
MethodPISA
Unit cell
Length a, b, c (Å)61.283, 93.872, 75.358
Angle α, β, γ (deg.)90.00, 93.08, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

#1: Protein L,D-transpeptidase 2 / LDT 2 / Ldt(Mt2)


Mass: 39532.004 Da / Num. of mol.: 2 / Fragment: residues 42-408
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (bacteria)
Strain: ATCC 25618 / H37Rv / Gene: ldtB, lppS, Rv2518c, RVBD_2518c, P425_02624 / Plasmid: pET28a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: I6Y9J2, Transferases; Acyltransferases; Aminoacyltransferases
#2: Chemical ChemComp-T8G / (2~{S},3~{R},4~{R})-4-(2-cyclohexyloxy-2-oxidanylidene-ethyl)sulfanyl-3-methyl-2-[(2~{S},3~{R})-3-oxidanyl-1-oxidanylidene-butan-2-yl]-3,4-dihydro-2~{H}-pyrrole-5-carboxylic acid


Mass: 385.475 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C18H27NO6S
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 397 / 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: 2.74 Å3/Da / Density % sol: 55.07 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / Details: PEG5000MME, Ammonium sulfate / PH range: 8

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.978 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Mar 16, 2015 / Details: mirrors
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.978 Å / Relative weight: 1
ReflectionResolution: 1.85→50 Å / Num. obs: 71306 / % possible obs: 99 % / Redundancy: 7.3 % / Rmerge(I) obs: 0.069 / Rpim(I) all: 0.027 / Rrim(I) all: 0.074 / Χ2: 0.915 / Net I/av σ(I): 23.844 / Net I/σ(I): 10.1 / Num. measured all: 517286
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allCC1/2Rpim(I) allRrim(I) allΧ2% possible all
1.85-1.887.20.45835100.9490.1810.4920.83197.8
1.88-1.927.20.38935240.9550.1540.4190.86298.2
1.92-1.957.20.34435090.9620.1360.3710.86198.3
1.95-1.997.20.28635300.9730.1130.3080.85498.1
1.99-2.047.20.23535660.9790.0930.2530.85198.5
2.04-2.087.20.2134840.9820.0830.2260.94498.5
2.08-2.147.30.17935630.9880.0710.1930.90998.7
2.14-2.197.30.16335360.9880.0640.1750.89198.8
2.19-2.267.30.14535490.9910.0570.1560.94498.7
2.26-2.337.30.12735510.9930.050.1370.92299
2.33-2.417.30.11435580.9940.0450.1220.90599.1
2.41-2.517.30.10135610.9940.040.1090.93399.1
2.51-2.637.30.09235780.9950.0360.0990.95199.2
2.63-2.767.30.08135950.9960.0320.0870.97299.4
2.76-2.947.30.07435750.9970.0290.0791.03899.6
2.94-3.167.30.06835980.9960.0270.0741.12499.6
3.16-3.487.30.0635980.9970.0240.0651.10199.7
3.48-3.997.10.04936120.9970.020.0520.95399.8
3.99-5.027.20.04136380.9980.0160.0440.76999.9
5.02-507.20.03836710.9970.0160.0410.67399.4

-
Phasing

PhasingMethod: molecular replacement

-
Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
HKL-2000data scaling
PHASERphasing
PDB_EXTRACT3.15data extraction
HKL-3000data reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3VYN

3vyn


Resolution: 1.852→37.243 Å / SU ML: 0.2 / Cross valid method: THROUGHOUT / σ(F): 1.38 / Phase error: 23.57 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2272 3509 4.92 %RANDOM
Rwork0.1967 ---
obs0.1982 71275 98.53 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.852→37.243 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5283 0 26 397 5706
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0085443
X-RAY DIFFRACTIONf_angle_d1.1217454
X-RAY DIFFRACTIONf_dihedral_angle_d12.7911894
X-RAY DIFFRACTIONf_chiral_restr0.05839
X-RAY DIFFRACTIONf_plane_restr0.005978
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.8525-1.87780.21671030.2042408X-RAY DIFFRACTION87
1.8778-1.90470.27661200.22052674X-RAY DIFFRACTION98
1.9047-1.93310.28031460.21342715X-RAY DIFFRACTION98
1.9331-1.96330.29621480.22072648X-RAY DIFFRACTION98
1.9633-1.99550.25331400.20782688X-RAY DIFFRACTION98
1.9955-2.02990.25391430.20342695X-RAY DIFFRACTION99
2.0299-2.06680.22361270.20412692X-RAY DIFFRACTION98
2.0668-2.10660.2221520.19562735X-RAY DIFFRACTION99
2.1066-2.14960.26121450.20162692X-RAY DIFFRACTION99
2.1496-2.19630.24811550.21062690X-RAY DIFFRACTION99
2.1963-2.24740.22941220.20892717X-RAY DIFFRACTION99
2.2474-2.30360.23021370.20612721X-RAY DIFFRACTION99
2.3036-2.36580.25931530.212732X-RAY DIFFRACTION99
2.3658-2.43540.2671230.21492727X-RAY DIFFRACTION99
2.4354-2.5140.24171610.21982687X-RAY DIFFRACTION99
2.514-2.60390.26891400.22562748X-RAY DIFFRACTION99
2.6039-2.70810.25441430.21872720X-RAY DIFFRACTION99
2.7081-2.83130.26861440.21742714X-RAY DIFFRACTION99
2.8313-2.98050.23431350.21712752X-RAY DIFFRACTION100
2.9805-3.16720.22541450.21842764X-RAY DIFFRACTION100
3.1672-3.41150.22581350.19432766X-RAY DIFFRACTION100
3.4115-3.75460.23051450.18482746X-RAY DIFFRACTION100
3.7546-4.29720.1971620.17362753X-RAY DIFFRACTION100
4.2972-5.41130.17931550.16032756X-RAY DIFFRACTION100
5.4113-37.25030.19191300.17692826X-RAY DIFFRACTION99

+
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://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