[English] 日本語
Yorodumi
- PDB-6i35: Crystal structure of human glycine decarboxylase (P-protein) boun... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6i35
TitleCrystal structure of human glycine decarboxylase (P-protein) bound with pyridoxyl-glycine-5'-monophosphate
ComponentsGlycine dehydrogenase (decarboxylating), mitochondrial
KeywordsOXIDOREDUCTASE / mitochondrial / glycine decarboxylase / glycine cleavage system P-protein
Function / homology
Function and homology information


response to methylamine / response to lipoic acid / glycine dehydrogenase (aminomethyl-transferring) / pyridoxal binding / glycine dehydrogenase (decarboxylating) activity / glycine catabolic process / Glycine degradation / glycine decarboxylation via glycine cleavage system / glycine cleavage complex / glycine binding ...response to methylamine / response to lipoic acid / glycine dehydrogenase (aminomethyl-transferring) / pyridoxal binding / glycine dehydrogenase (decarboxylating) activity / glycine catabolic process / Glycine degradation / glycine decarboxylation via glycine cleavage system / glycine cleavage complex / glycine binding / cellular response to leukemia inhibitory factor / pyridoxal phosphate binding / electron transfer activity / lyase activity / mitochondrial matrix / protein homodimerization activity / mitochondrion / nucleoplasm / plasma membrane
Similarity search - Function
Glycine dehydrogenase (decarboxylating) / Glycine cleavage system P protein / : / : / Glycine cleavage system P-protein / Glycine dehydrogenase, C-terminal domain / Aromatic amino acid beta-eliminating lyase/threonine aldolase / Beta-eliminating lyase / Pyridoxal phosphate-dependent transferase, small domain / Pyridoxal phosphate-dependent transferase, major domain / Pyridoxal phosphate-dependent transferase
Similarity search - Domain/homology
BICARBONATE ION / DI(HYDROXYETHYL)ETHER / Chem-PLG / Glycine dehydrogenase (decarboxylating), mitochondrial
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsVan Laer, B. / Kapp, U. / Leonard, G. / Mueller-Dieckmann, C.
CitationJournal: To Be Published
Title: Structural insights in human glycine decarboxylase and comparison with the Neanderthal variant
Authors: Van Laer, B. / Kapp, U. / Signor, L. / Leonard, G. / Mueller-Dieckmann, C.
History
DepositionNov 5, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 20, 2019Provider: repository / Type: Initial release
Revision 1.1Jan 24, 2024Group: 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 / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Glycine dehydrogenase (decarboxylating), mitochondrial
B: Glycine dehydrogenase (decarboxylating), mitochondrial
C: Glycine dehydrogenase (decarboxylating), mitochondrial
D: Glycine dehydrogenase (decarboxylating), mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)440,46822
Polymers438,0494
Non-polymers2,41918
Water18,4471024
1
A: Glycine dehydrogenase (decarboxylating), mitochondrial
B: Glycine dehydrogenase (decarboxylating), mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)220,20411
Polymers219,0242
Non-polymers1,1809
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9640 Å2
ΔGint-3 kcal/mol
Surface area57290 Å2
MethodPISA
2
C: Glycine dehydrogenase (decarboxylating), mitochondrial
D: Glycine dehydrogenase (decarboxylating), mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)220,26411
Polymers219,0242
Non-polymers1,2399
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9810 Å2
ΔGint6 kcal/mol
Surface area57330 Å2
MethodPISA
Unit cell
Length a, b, c (Å)85.660, 123.440, 197.670
Angle α, β, γ (deg.)90.00, 97.93, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13A
23D
14B
24C
15B
25D
16C
26D

NCS domain segments:

Component-ID: _ / Refine code: _

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ARGARGPROPROAA51 - 10048 - 961
21ARGARGPROPROBB51 - 10048 - 961
12ALAALAMETMETAA49 - 10056 - 962
22ALAALAMETMETCC49 - 10056 - 962
13ARGARGPROPROAA51 - 10048 - 961
23ARGARGPROPRODD51 - 10048 - 961
14ARGARGPROPROBB51 - 10048 - 961
24ARGARGPROPROCC51 - 10048 - 961
15ARGARGPROPROBB51 - 10048 - 961
25ARGARGPROPRODD51 - 10048 - 961
16ARGARGPROPROCC51 - 10048 - 961
26ARGARGPROPRODD51 - 10048 - 961

NCS ensembles :
ID
1
2
3
4
5
6

-
Components

-
Protein , 1 types, 4 molecules ABCD

#1: Protein
Glycine dehydrogenase (decarboxylating), mitochondrial / Glycine cleavage system P protein / Glycine decarboxylase / Glycine dehydrogenase (aminomethyl-transferring)


Mass: 109512.203 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: GLDC, GCSP / Production host: Escherichia coli BL21(DE3) (bacteria)
References: UniProt: P23378, glycine dehydrogenase (aminomethyl-transferring)

-
Non-polymers , 6 types, 1042 molecules

#2: Chemical
ChemComp-PLG / N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE] / N-PYRIDOXYL-GLYCINE-5-MONOPHOSPHATE


Mass: 306.209 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H15N2O7P / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H6O2
#4: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical ChemComp-BCT / BICARBONATE ION


Mass: 61.017 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: CHO3 / Comment: pH buffer*YM
#6: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C4H10O3
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1024 / 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: 2.38 Å3/Da / Density % sol: 48 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 / Details: 0.1 M HEPES pH 7, 6 % PEG3350, 10 mM DTT

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: MASSIF-3 / Wavelength: 0.97 Å
DetectorType: DECTRIS EIGER X 4M / Detector: PIXEL / Date: Sep 14, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97 Å / Relative weight: 1
ReflectionResolution: 2→49.33 Å / Num. obs: 271538 / % possible obs: 99 % / Redundancy: 4.6 % / CC1/2: 0.995 / Rrim(I) all: 0.17 / Net I/σ(I): 5.3
Reflection shellResolution: 2→2.1 Å / Redundancy: 4.5 % / Mean I/σ(I) obs: 1.1 / Num. unique obs: 36741 / CC1/2: 0.484 / % possible all: 98.8

-
Processing

Software
NameVersionClassification
REFMAC5.8.0230refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6I33
Resolution: 2→49.33 Å / Cor.coef. Fo:Fc: 0.967 / Cor.coef. Fo:Fc free: 0.955 / Cross valid method: THROUGHOUT / ESU R: 0.211 / ESU R Free: 0.17 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.24047 13576 5 %RANDOM
Rwork0.215 ---
obs0.21627 257933 98.99 %-
Solvent computationIon probe radii: 0.7 Å / Shrinkage radii: 0.7 Å / VDW probe radii: 1 Å
Displacement parametersBiso mean: 47.125 Å2
Baniso -1Baniso -2Baniso -3
1--2.71 Å20 Å22.96 Å2
2--0.75 Å20 Å2
3---1.1 Å2
Refinement stepCycle: 1 / Resolution: 2→49.33 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms29750 0 158 1024 30932
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.01430560
X-RAY DIFFRACTIONr_bond_other_d0.0010.01727388
X-RAY DIFFRACTIONr_angle_refined_deg1.3411.65941354
X-RAY DIFFRACTIONr_angle_other_deg1.4451.63764346
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.73353808
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.21421.9051596
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.713155210
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.06415216
X-RAY DIFFRACTIONr_chiral_restr0.0820.23949
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.0234432
X-RAY DIFFRACTIONr_gen_planes_other0.0110.025456
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.1341.82615262
X-RAY DIFFRACTIONr_mcbond_other1.1341.82615263
X-RAY DIFFRACTIONr_mcangle_it1.8022.73219060
X-RAY DIFFRACTIONr_mcangle_other1.8032.73319061
X-RAY DIFFRACTIONr_scbond_it1.4532.02115298
X-RAY DIFFRACTIONr_scbond_other1.452.0215295
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other2.2522.95822292
X-RAY DIFFRACTIONr_long_range_B_refined5.24122.2834499
X-RAY DIFFRACTIONr_long_range_B_other5.2422.12534371
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A323310.08
12B323310.08
21A327610.06
22C327610.06
31A322460.08
32D322460.08
41B323500.07
42C323500.07
51B326220.06
52D326220.06
61C322920.07
62D322920.07
LS refinement shellResolution: 2→2.052 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.402 991 -
Rwork0.389 18832 -
obs--98.22 %
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)
10.77730.0784-0.08040.9822-0.06860.66560.04710.10190.0294-0.06840.0163-0.1204-0.02950.1015-0.06340.29050.0137-0.25130.0333-0.02090.274618.519-23.069-4.741
21.19420.11020.44581.1517-0.35761.61110.02290.2624-0.0795-0.27020.07510.15720.1117-0.1094-0.09790.35150.001-0.30560.0878-0.01750.2771-1.86-33.866-13.723
30.8591-0.1867-0.25512.68320.46230.82480.11360.07240.185-0.0571-0.06120.4181-0.1654-0.183-0.05240.24770.042-0.15530.04750.03450.3292-14.941-15.4717.432
43.5680.7227-2.85561.1469-0.33393.43550.1094-0.13950.14290.2304-0.04050.1115-0.2672-0.0505-0.0690.34860.0427-0.16790.0299-0.01870.321-2.54-2.51912.287
50.75180.00230.07111.1022-0.13420.81330.0691-0.270.00190.4517-0.0174-0.16040.01460.141-0.05180.5387-0.0015-0.34730.1736-0.03190.25320.934-32.12237.749
61.0464-0.0892-0.02542.94360.32991.10920.0507-0.2773-0.17120.4720.03930.00230.18140.0024-0.09010.46-0.0035-0.26720.14920.06280.208311.243-46.28434.344
70.66670.21640.10951.0044-0.06770.68670.0727-0.27690.10540.471-0.0461-0.2237-0.11670.2082-0.02650.5382-0.0541-0.3630.2251-0.07450.316428.615-19.29738.547
81.46030.08680.63034.5534-1.31311.5763-0.0489-0.27180.28030.55770.14950.2225-0.295-0.1815-0.10070.53040.0178-0.14220.1717-0.12550.31863.335-2.82533.871
90.7556-0.0973-0.02910.97430.02030.71960.0619-0.15450.0310.1016-0.00060.0387-0.0094-0.0365-0.06130.2974-0.0317-0.25320.03560.01240.2524-26.22334.184105.116
101.9314-2.16452.08952.4509-2.35992.28970.0307-0.1159-0.0827-0.06570.05760.02530.1288-0.0656-0.08840.42010.0543-0.07450.31580.0870.403-31.11320.662114.632
111.10080.3746-0.43941.4915-0.4880.63030.1662-0.1360.13160.004-0.1087-0.3483-0.13050.1919-0.05760.337-0.0459-0.21850.0599-0.02990.4144-2.71540.64992.41
123.6328-0.9403-2.95851.25340.52083.21390.10110.15790.1668-0.2638-0.0721-0.1122-0.27070.0105-0.0290.361-0.0348-0.16560.03130.0220.3114-10.96757.16185.608
130.5930.1868-0.00861.0952-0.17661.21160.0684-0.03360.1416-0.16290.04160.5637-0.1768-0.3937-0.11010.38260.0544-0.34180.21640.05330.541-53.69543.02277.343
140.9912-0.09650.16261.71520.20350.90670.11020.3254-0.1338-0.5722-0.04730.04190.08980.0427-0.0630.57430.0515-0.30090.1464-0.03130.2376-25.67417.78357.65
150.7724-0.24260.15051.03330.02960.66360.0950.26530.0895-0.5246-0.07070.244-0.1195-0.1588-0.02430.58280.0679-0.37590.1790.06020.3217-42.00840.42859.186
161.6424-0.17810.5714.9491.62211.6595-0.01150.24970.2307-0.61740.1109-0.1466-0.28590.2222-0.09940.5174-0.0052-0.14050.16030.13260.3176-16.72556.92863.981
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A49 - 591
2X-RAY DIFFRACTION2A592 - 823
3X-RAY DIFFRACTION3A824 - 958
4X-RAY DIFFRACTION4A959 - 1005
5X-RAY DIFFRACTION5B51 - 340
6X-RAY DIFFRACTION6B341 - 506
7X-RAY DIFFRACTION7B507 - 940
8X-RAY DIFFRACTION8B941 - 1004
9X-RAY DIFFRACTION9C49 - 781
10X-RAY DIFFRACTION10C782 - 790
11X-RAY DIFFRACTION11C794 - 958
12X-RAY DIFFRACTION12C959 - 1005
13X-RAY DIFFRACTION13D51 - 130
14X-RAY DIFFRACTION14D131 - 506
15X-RAY DIFFRACTION15D507 - 940
16X-RAY DIFFRACTION16D941 - 1004

+
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