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- PDB-6php: Crystal structure of glucagon analog with 4-bromo-phenylalanine s... -

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Basic information

Entry
Database: PDB / ID: 6php
TitleCrystal structure of glucagon analog with 4-bromo-phenylalanine substitutions at position 6 and 22 in space group I41 at 1.65 A resolution
ComponentsGlucagon
KeywordsHORMONE / glucagon / GPCR ligand / peptide hormone
Function / homology
Function and homology information


glucagon receptor binding / protein kinase A signaling / negative regulation of execution phase of apoptosis / feeding behavior / positive regulation of calcium ion import / positive regulation of insulin secretion involved in cellular response to glucose stimulus / Synthesis, secretion, and deacylation of Ghrelin / positive regulation of gluconeogenesis / regulation of insulin secretion / cellular response to glucagon stimulus ...glucagon receptor binding / protein kinase A signaling / negative regulation of execution phase of apoptosis / feeding behavior / positive regulation of calcium ion import / positive regulation of insulin secretion involved in cellular response to glucose stimulus / Synthesis, secretion, and deacylation of Ghrelin / positive regulation of gluconeogenesis / regulation of insulin secretion / cellular response to glucagon stimulus / response to activity / gluconeogenesis / hormone activity / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / adenylate cyclase-activating G protein-coupled receptor signaling pathway / Glucagon signaling in metabolic regulation / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / Glucagon-type ligand receptors / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / glucose homeostasis / G alpha (s) signalling events / secretory granule lumen / G alpha (q) signalling events / positive regulation of ERK1 and ERK2 cascade / G protein-coupled receptor signaling pathway / receptor ligand activity / endoplasmic reticulum lumen / signaling receptor binding / negative regulation of apoptotic process / extracellular space / extracellular region / identical protein binding / plasma membrane
Similarity search - Function
Glucagon / Glucagon/GIP/secretin/VIP / Peptide hormone / Glucagon / GIP / secretin / VIP family signature. / Glucagon like hormones
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.65 Å
AuthorsMroz, P.A. / Gonzalez-Gutierrez, G. / DiMarchi, R.D.
Funding support United States, 1items
OrganizationGrant numberCountry
Other governmentIndiana University Internal grant United States
Citation
Journal: To Be Published
Title: High resolution X-ray structure of glucagon and selected stereo-inversed analogs in novel crystallographic packing arrangement.
Authors: Mroz, P.A. / Gonzalez-Gutierrez, G. / DiMarchi, R.D.
#1: Journal: Acta Crystallogr D Biol Crystallogr / Year: 2010
Title: PHENIX: a comprehensive Python-based system for macromolecular structure solution.
Authors: Paul D Adams / Pavel V Afonine / Gábor Bunkóczi / Vincent B Chen / Ian W Davis / Nathaniel Echols / Jeffrey J Headd / Li-Wei Hung / Gary J Kapral / Ralf W Grosse-Kunstleve / Airlie J McCoy ...Authors: Paul D Adams / Pavel V Afonine / Gábor Bunkóczi / Vincent B Chen / Ian W Davis / Nathaniel Echols / Jeffrey J Headd / Li-Wei Hung / Gary J Kapral / Ralf W Grosse-Kunstleve / Airlie J McCoy / Nigel W Moriarty / Robert Oeffner / Randy J Read / David C Richardson / Jane S Richardson / Thomas C Terwilliger / Peter H Zwart /
Abstract: Macromolecular X-ray crystallography is routinely applied to understand biological processes at a molecular level. However, significant time and effort are still required to solve and complete many ...Macromolecular X-ray crystallography is routinely applied to understand biological processes at a molecular level. However, significant time and effort are still required to solve and complete many of these structures because of the need for manual interpretation of complex numerical data using many software packages and the repeated use of interactive three-dimensional graphics. PHENIX has been developed to provide a comprehensive system for macromolecular crystallographic structure solution with an emphasis on the automation of all procedures. This has relied on the development of algorithms that minimize or eliminate subjective input, the development of algorithms that automate procedures that are traditionally performed by hand and, finally, the development of a framework that allows a tight integration between the algorithms.
History
DepositionJun 25, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 1, 2020Provider: repository / Type: Initial release
Revision 2.0Nov 15, 2023Group: Atomic model / Data collection / Database references
Category: atom_site / chem_comp_atom ...atom_site / chem_comp_atom / chem_comp_bond / database_2
Item: _atom_site.auth_atom_id / _atom_site.label_atom_id ..._atom_site.auth_atom_id / _atom_site.label_atom_id / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Glucagon


Theoretical massNumber of molelcules
Total (without water)3,6451
Polymers3,6451
Non-polymers00
Water25214
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: mass spectrometry
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area0 Å2
ΔGint0 kcal/mol
Surface area2660 Å2
MethodPISA
Unit cell
Length a, b, c (Å)41.712, 41.712, 30.434
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number80
Space group name H-MI41
Components on special symmetry positions
IDModelComponents
11A-114-

HOH

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Components

#1: Protein/peptide Glucagon


Mass: 3644.573 Da / Num. of mol.: 1 / Fragment: UNP residues 53-81 / Mutation: F6BrF, F22BrF / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P01275
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 14 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

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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: 1.82 Å3/Da / Density % sol: 32.27 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop
Details: Tacsimate, pH 4, 16% PEG3350, 0.1 M sodium acetate, pH 4.6

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 4.2.2 / Wavelength: 0.9184 Å
DetectorType: RDI CMOS_8M / Detector: CMOS / Date: May 17, 2018
RadiationMonochromator: double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9184 Å / Relative weight: 1
ReflectionResolution: 1.65→29.49 Å / Num. obs: 3194 / % possible obs: 99.7 % / Redundancy: 6.6 % / CC1/2: 0.996 / Rpim(I) all: 0.042 / Rrim(I) all: 0.11 / Rsym value: 0.102 / Net I/σ(I): 10.7
Reflection shellResolution: 1.65→2.01 Å / Mean I/σ(I) obs: 1.1 / Num. unique obs: 1267 / CC1/2: 0.784 / Rpim(I) all: 0.51 / Rrim(I) all: 1.32 / Rsym value: 1.216

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Processing

Software
NameVersionClassification
PHENIX(1.14_3260: ???)refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: SAD / Resolution: 1.65→29.49 Å / SU ML: 0.23 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 20.89
RfactorNum. reflection% reflection
Rfree0.2458 143 4.67 %
Rwork0.225 --
obs0.2266 3060 95.65 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 1.65→29.49 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms211 0 0 14 225
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.018223
X-RAY DIFFRACTIONf_angle_d1.556303
X-RAY DIFFRACTIONf_dihedral_angle_d3.032171
X-RAY DIFFRACTIONf_chiral_restr0.06430
X-RAY DIFFRACTIONf_plane_restr0.01238
LS refinement shellResolution: 1.6503→1.68 Å /
Num. reflection% reflection
Rwork2917 -
obs-96 %

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