1zsg

beta PIX-SH3 complexed with an atypical peptide from alpha-PAK

Method: SOLUTION NMR D_max: 56.1 Å Quality: GOOD

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Rho guanine nucleotide exchange factor 7

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 179–243	Fragment：sequence database residues 179-243	Serine/threonine-protein kinase PAK 1 × 1 （Q13153）	SOLUTION NMR NMR measurement conditions：pH 7.3；298 K；Ionic strength (raw mmCIF value) 100 mM Na2SO4；Pressure 1 NMR measurement conditions：pH 7.3；298 K；Ionic strength (raw mmCIF value) 100 mM Na2SO4；Pressure 1 NMR sample composition：1mM 15N labelled PIX-SH3 complexed with 1.2 mM peptide in 20 mM Na2HPO4/NaH2PO4, pH 7.3, 100mM Na2SO4, 0.05% NaN3, 90% H2O, 10% D2O \| 90% H2O/10% D2O NMR sample composition：1mM 15N,13C labelled PIX-SH3 complexed with 1.2 mM peptide in 20 mM Na2HPO4/NaH2PO4, pH 7.3, 100mM Na2SO4, 0.05% NaN3, 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1ZSG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BY1 DBL homology domain from beta-PIX Deposited 1998-10-22	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–289（209 aa） Fragment：DBL HOMOLOGY DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；311 K；Ionic strength (raw mmCIF value) 150mM；Pressure 1 NMR sample composition 90% H2O/10% D2O	Resolution not provided
2L3G Solution NMR Structure of CH domain of Rho guanine nucleotide exchange factor 7 from Homo sapiens, Northeast Structural Genomics Consortium Target HR4495E Deposited 2010-09-13	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–137（137 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Pressure ambient NMR sample composition 0.87 mM [U-100% 13C; U-100% 15N] HR4495E, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.85 mM [U-5% 13C; U-100% 15N] HR4495E, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
5SXP STRUCTURAL BASIS FOR THE INTERACTION BETWEEN ITCH PRR AND BETA-PIX Deposited 2016-08-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 183–243（61 aa） Fragment：UNP residues 183-243 Chain C 183–243（61 aa） Fragment：UNP residues 183-243	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；100 mM MIB buffer pH 5.0 and 25% PEG1500	Resolution 1.65 Å R-free 0.161
5SXP STRUCTURAL BASIS FOR THE INTERACTION BETWEEN ITCH PRR AND BETA-PIX Deposited 2016-08-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 183–243（61 aa） Fragment：UNP residues 183-243 Chain D 183–243（61 aa） Fragment：UNP residues 183-243	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；100 mM MIB buffer pH 5.0 and 25% PEG1500	Resolution 1.65 Å R-free 0.161

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ARHG7_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–65； UniProt 179–243

Serine/threonine-protein kinase PAK 1

OrganismNot specified

UniProt Q13153

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 183–204	Fragment：sequence database residues 183-204	Rho guanine nucleotide exchange factor 7 × 1 （Q14155）	SOLUTION NMR NMR measurement conditions：pH 7.3；298 K；Ionic strength (raw mmCIF value) 100 mM Na2SO4；Pressure 1 NMR measurement conditions：pH 7.3；298 K；Ionic strength (raw mmCIF value) 100 mM Na2SO4；Pressure 1 NMR sample composition：1mM 15N labelled PIX-SH3 complexed with 1.2 mM peptide in 20 mM Na2HPO4/NaH2PO4, pH 7.3, 100mM Na2SO4, 0.05% NaN3, 90% H2O, 10% D2O \| 90% H2O/10% D2O NMR sample composition：1mM 15N,13C labelled PIX-SH3 complexed with 1.2 mM peptide in 20 mM Na2HPO4/NaH2PO4, pH 7.3, 100mM Na2SO4, 0.05% NaN3, 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 1ZSG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1F3M CRYSTAL STRUCTURE OF HUMAN SERINE/THREONINE KINASE PAK1 Deposited 2000-06-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 70–149（80 aa） Fragment：PAK1 AUTOREGULATORY DOMAIN (70-149) Chain B 70–149（80 aa） Fragment：PAK1 AUTOREGULATORY DOMAIN (70-149) Chain C 249–545（297 aa） Fragment：KINASE DOMAIN (249-545) Chain D 249–545（297 aa） Fragment：KINASE DOMAIN (249-545)	Mutation：K299R Mutation：K299R	IOD IODIDE ION × 28	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；285 K；Ammonium Sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 285K	Resolution 2.30 Å R-free 0.258
1YHV Crystal Structure of PAK1 kinase domain with two point mutations (K299R, T423E) Deposited 2005-01-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa） Fragment：kinase domain	Mutation：K299R, T423E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG 4000, NaCl, PIPES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 1.80 Å R-free 0.240
1YHW Crystal Structure of PAK1 kinase domain with one point mutations (K299R) Deposited 2005-01-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa） Fragment：kinase domain	Mutation：K299R	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG 4000, NaCl, PIPES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.80 Å R-free 0.243
28OQ Protein Kinaze domain PAK1 complexed with NVS inhibitor Deposited 2026-02-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 249–545（297 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292 K；0.1 M HEPES pH 7.5, 0.2 M ammonium sulfate , 24 % (w/v) PEG 1357 3350	Resolution 2.28 Å R-free 0.266
28OQ Protein Kinaze domain PAK1 complexed with NVS inhibitor Deposited 2026-02-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	CL CHLORIDE ION × 1 A1JZR (3~{S})-3-[(~{Z})-[11-[2,2-bis(fluoranyl)ethyl]-8-chloranyl-3-fluoranyl-5~{H}-benzo[b][1,4]benzodiazepin-6-ylidene]amino]-~{N}-propan-2-yl-pyrrolidine-1-carboxamide × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292 K；0.1 M HEPES pH 7.5, 0.2 M ammonium sulfate , 24 % (w/v) PEG 1357 3350	Resolution 2.28 Å R-free 0.266
2HY8 PAK1 complex with ST2001 Deposited 2006-08-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain 1 249–545（297 aa） Fragment：kinase domain (residues 249-545)	Mutation：K299R, T423E	1ST (5S,6R,7R,9R)-12-HYDROXY-6-METHOXY-5-METHYL-7-(METHYLAMINO)-6,7,8,9-TETRAHYDRO-5H,14H-5,9-EPOXY-4B,9A,15-TRIAZADIBENZO[ B,H]CYCLONONA[1,2,3,4-JKL]CYCLOPENTA[E]-AS-INDACEN-14-ONE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；1:1 ration of protein and precipitant. Precipitant: 0.13 M PIPES pH 6.5, 1.5 M NaCl, 23% PEG 4000, 10 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.234
2QME Crystal structure of human RAC3 in complex with CRIB domain of human p21-activated kinase 1 (PAK1) Deposited 2007-07-16	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain I 74–109（36 aa） Fragment：CRIB domain	Not recorded	MG MAGNESIUM ION × 1 GCP PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.1 M Tris-HCl pH 8.5, 2 M (NH4)2S04, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.75 Å R-free 0.192
2QME Crystal structure of human RAC3 in complex with CRIB domain of human p21-activated kinase 1 (PAK1) Deposited 2007-07-16	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain I 74–109（36 aa） Fragment：CRIB domain	Not recorded	MG MAGNESIUM ION × 2 GCP PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 2 GOL GLYCEROL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.1 M Tris-HCl pH 8.5, 2 M (NH4)2S04, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.75 Å R-free 0.192
3DVP Pak1 peptide bound LC8 Deposited 2008-07-18	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 212–221（10 aa） Chain D 212–221（10 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；100 mM MES, 200 mM NaCl, 27% (w/v) PEG 4000, and 10% 0.1 M (NH4)6CoCl3, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 273K, temperature 293K	Resolution 2.50 Å R-free 0.263
3FXZ Crystal structure of PAK1 kinase domain with ruthenium complex lambda-FL172 Deposited 2009-01-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa） Fragment：UNP residues 249-545	Mutation：K299R Non-standard monomer：Yes (specific site not provided by mmCIF)	FLL OCTAHEDRAL RU-PYRIDOCARBAZOLE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；277 K；0.1M Tris pH 8.0, 1M NaCl, 25% PEG 4000, 10mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.64 Å R-free 0.218
3FY0 Crystal structure of PAK1 kinase domain with ruthenium complex DW1 Deposited 2009-01-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa） Fragment：UNP residues 249-545	Mutation：K299R Non-standard monomer：Yes (specific site not provided by mmCIF)	DW1 Ruthenium pyridocarbazole × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M HEPES pH 7.5, 1M NaCl, 25% PEG 10000, 10mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.35 Å R-free 0.260
3Q4Z Structure of unphosphorylated PAK1 kinase domain Deposited 2010-12-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 248–545（298 aa） Fragment：kinase domain, UNP residues 248-545 Chain B 248–545（298 aa） Fragment：kinase domain, UNP residues 248-545	Mutation：S259I, K299R, D389N, L516I Mutation：S259I, K299R, D389N, L516I	MG MAGNESIUM ION × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；0.1M Hepes pH 7.5, 25% PEG 3350, 0.2M Ammonium Sulphate, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 1.89 Å R-free 0.231
3Q52 Structure of phosphorylated PAK1 kinase domain Deposited 2010-12-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 248–545（298 aa） Fragment：kinase domain, UNP residues 248-545	Mutation：K299R, L516I Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；294 K；25% PEG 3350, 0.2M Na/K Tartrate, 0.1M NDSB256, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 1.80 Å R-free 0.214
3Q53 Structure of phosphorylated PAK1 kinase domain in complex with ATP Deposited 2010-12-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 248–545（298 aa） Fragment：kinase domain, UNP residues 248-545	Mutation：K299R, L516I Non-standard monomer：Yes (specific site not provided by mmCIF)	ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；294 K；25% PEG 3350, 0.2M Na/K Tartrate, 0.1M NDSB256, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.09 Å R-free 0.223
4DAW Crystal structure of PAK1 kinase domain with the ruthenium phthalimide complex Deposited 2012-01-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa） Fragment：unp residues 249-545	Mutation：K299R Non-standard monomer：Yes (specific site not provided by mmCIF)	0H2 [1,3-dioxo-6-(pyridin-2-yl-kappaN)-2,3-dihydro-1H-isoindol-5-yl-kappaC~5~][(thioxomethylidene)azanido-kappaN](1,4,7-trithionane-kappa~3~S~1~,S~4~,S~7~)ruthenium × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；25 PEG 4000, 1 M NaCl, 10 mM DTT, 0.1 M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.238
4EQC Crystal structure of PAK1 kinase domain in complex with FRAX597 inhibitor Deposited 2012-04-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa） Fragment：unp residues 249-545	Mutation：K299R Non-standard monomer：Yes (specific site not provided by mmCIF)	XR1 6-[2-chloro-4-(1,3-thiazol-5-yl)phenyl]-8-ethyl-2-{[4-(4-methylpiperazin-1-yl)phenyl]amino}pyrido[2,3-d]pyrimidin-7(8H)-one × 1 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；0.1 M HEPES, 1 M NaCl, 25% PEG 3350, 10 mM DTT, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.01 Å R-free 0.253
4O0R Back pocket flexibility provides group-II PAK selectivity for type 1 kinase inhibitors Deposited 2013-12-14	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa） Fragment：unp residues 249-545	Not recorded	7KC PF-3758309 × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；292 K；crystals were grown at 19 C from 1.0 uL + 1.0 uL vapor diffusion drops containing 10 mg/mL protein, 1 mM ligand, 0.15 M DL-Malic Acid, 20% - 30% PEG 3350, 4% 1,3-Propanediol and 0.1 M Sodium Malonate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 292K	Resolution 2.40 Å R-free 0.242
4O0R Back pocket flexibility provides group-II PAK selectivity for type 1 kinase inhibitors Deposited 2013-12-14	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 249–545（297 aa） Fragment：unp residues 249-545	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；292 K；crystals were grown at 19 C from 1.0 uL + 1.0 uL vapor diffusion drops containing 10 mg/mL protein, 1 mM ligand, 0.15 M DL-Malic Acid, 20% - 30% PEG 3350, 4% 1,3-Propanediol and 0.1 M Sodium Malonate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 292K	Resolution 2.40 Å R-free 0.242
4O0R Back pocket flexibility provides group-II PAK selectivity for type 1 kinase inhibitors Deposited 2013-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 249–545（297 aa） Fragment：unp residues 249-545 Chain B 249–545（297 aa） Fragment：unp residues 249-545	Not recorded	7KC PF-3758309 × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；292 K；crystals were grown at 19 C from 1.0 uL + 1.0 uL vapor diffusion drops containing 10 mg/mL protein, 1 mM ligand, 0.15 M DL-Malic Acid, 20% - 30% PEG 3350, 4% 1,3-Propanediol and 0.1 M Sodium Malonate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 292K	Resolution 2.40 Å R-free 0.242
4O0T Back pocket flexibility provides group-II PAK selectivity for type 1 kinase inhibitors Deposited 2013-12-14	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa） Fragment：unp residues 249-545	Not recorded	2OL 1-({1-(2-aminopyrimidin-4-yl)-2-[(2-methoxyethyl)amino]-1H-benzimidazol-6-yl}ethynyl)cyclohexanol × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；292 K；crystals were grown at 19 C from 1.0 uL + 1.0 uL vapor diffusion drops containing 10 mg/mL protein, 1 mM ligand, 0.15 M DL-Malic Acid pH 7.0, 20% - 30% PEG 3350, 4% 1,3-Propanediol and 0.1 M Sodium Malonate, VAPOR DIFFUSION, SITTING DROP, temperature 292K	Resolution 2.60 Å R-free 0.265
4O0T Back pocket flexibility provides group-II PAK selectivity for type 1 kinase inhibitors Deposited 2013-12-14	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 249–545（297 aa） Fragment：unp residues 249-545	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；292 K；crystals were grown at 19 C from 1.0 uL + 1.0 uL vapor diffusion drops containing 10 mg/mL protein, 1 mM ligand, 0.15 M DL-Malic Acid pH 7.0, 20% - 30% PEG 3350, 4% 1,3-Propanediol and 0.1 M Sodium Malonate, VAPOR DIFFUSION, SITTING DROP, temperature 292K	Resolution 2.60 Å R-free 0.265
4O0T Back pocket flexibility provides group-II PAK selectivity for type 1 kinase inhibitors Deposited 2013-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 249–545（297 aa） Fragment：unp residues 249-545 Chain B 249–545（297 aa） Fragment：unp residues 249-545	Not recorded	2OL 1-({1-(2-aminopyrimidin-4-yl)-2-[(2-methoxyethyl)amino]-1H-benzimidazol-6-yl}ethynyl)cyclohexanol × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；292 K；crystals were grown at 19 C from 1.0 uL + 1.0 uL vapor diffusion drops containing 10 mg/mL protein, 1 mM ligand, 0.15 M DL-Malic Acid pH 7.0, 20% - 30% PEG 3350, 4% 1,3-Propanediol and 0.1 M Sodium Malonate, VAPOR DIFFUSION, SITTING DROP, temperature 292K	Resolution 2.60 Å R-free 0.265
4P90 Crystal structure of the kinase domain of human PAK1 in complex with compound 15 Deposited 2014-04-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa）	Mutation：D389N, T423E, E503D	2K0 [2-chloro-5-(hydroxymethyl)phenyl]{5-[1-(piperidin-4-yl)-1H-pyrazol-4-yl]-1H-pyrrolo[2,3-b]pyridin-3-yl}methanone × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.6；293 K；0.2M ammonium sulphate, 16% PEG 3350, 0.1M Hepes (pH 7.6)	Resolution 2.49 Å R-free 0.225
4P90 Crystal structure of the kinase domain of human PAK1 in complex with compound 15 Deposited 2014-04-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 249–545（297 aa）	Mutation：D389N, T423E, E503D	2K0 [2-chloro-5-(hydroxymethyl)phenyl]{5-[1-(piperidin-4-yl)-1H-pyrazol-4-yl]-1H-pyrrolo[2,3-b]pyridin-3-yl}methanone × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.6；293 K；0.2M ammonium sulphate, 16% PEG 3350, 0.1M Hepes (pH 7.6)	Resolution 2.49 Å R-free 0.225
4ZJI PAK1 in complex with 2-chloro-5-ethyl-8-fluoro-11-(4-methylpiperazin-1-yl)-dibenzodiazepine Deposited 2015-04-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa）	Not recorded	4OQ 2-chloro-5-ethyl-8-fluoro-11-(4-methylpiperazin-1-yl)-dibenzodiazepine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；Equal volumes (1.0 uL) of reservoir solution and protein solution were mixed. Reservoir solution: 17.2% (w/v) PEG3350, 0.2 M magnesium formate (dihydrate)	Resolution 1.99 Å R-free 0.220
4ZJI PAK1 in complex with 2-chloro-5-ethyl-8-fluoro-11-(4-methylpiperazin-1-yl)-dibenzodiazepine Deposited 2015-04-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 249–545（297 aa）	Not recorded	4OQ 2-chloro-5-ethyl-8-fluoro-11-(4-methylpiperazin-1-yl)-dibenzodiazepine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；Equal volumes (1.0 uL) of reservoir solution and protein solution were mixed. Reservoir solution: 17.2% (w/v) PEG3350, 0.2 M magnesium formate (dihydrate)	Resolution 1.99 Å R-free 0.220
4ZJI PAK1 in complex with 2-chloro-5-ethyl-8-fluoro-11-(4-methylpiperazin-1-yl)-dibenzodiazepine Deposited 2015-04-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 249–545（297 aa）	Not recorded	4OQ 2-chloro-5-ethyl-8-fluoro-11-(4-methylpiperazin-1-yl)-dibenzodiazepine × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；Equal volumes (1.0 uL) of reservoir solution and protein solution were mixed. Reservoir solution: 17.2% (w/v) PEG3350, 0.2 M magnesium formate (dihydrate)	Resolution 1.99 Å R-free 0.220
4ZJI PAK1 in complex with 2-chloro-5-ethyl-8-fluoro-11-(4-methylpiperazin-1-yl)-dibenzodiazepine Deposited 2015-04-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 249–545（297 aa）	Not recorded	4OQ 2-chloro-5-ethyl-8-fluoro-11-(4-methylpiperazin-1-yl)-dibenzodiazepine × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；Equal volumes (1.0 uL) of reservoir solution and protein solution were mixed. Reservoir solution: 17.2% (w/v) PEG3350, 0.2 M magnesium formate (dihydrate)	Resolution 1.99 Å R-free 0.220
4ZJJ PAK1 in complex with (S)-N-(tert-butyl)-3-((2-chloro-5-ethyl-8-fluoro-dibenzodiazepin-11-yl)amino)pyrrolidine-1-carboxamide Deposited 2015-04-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa）	Not recorded	4OR (S)-N-(tert-butyl)-3-((2-chloro-5-ethyl-8-fluoro-dibenzodiazepin-11-yl)amino)pyrrolidine-1-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；Equal volumes (0.8 uL) of reservoir solution and protein solution were mixed. Reservoir solution: 16.8% (w/v) PEG3350, 0.2 M magnesium formate (dihydrate)	Resolution 2.20 Å R-free 0.238
4ZJJ PAK1 in complex with (S)-N-(tert-butyl)-3-((2-chloro-5-ethyl-8-fluoro-dibenzodiazepin-11-yl)amino)pyrrolidine-1-carboxamide Deposited 2015-04-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 249–545（297 aa）	Not recorded	4OR (S)-N-(tert-butyl)-3-((2-chloro-5-ethyl-8-fluoro-dibenzodiazepin-11-yl)amino)pyrrolidine-1-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；Equal volumes (0.8 uL) of reservoir solution and protein solution were mixed. Reservoir solution: 16.8% (w/v) PEG3350, 0.2 M magnesium formate (dihydrate)	Resolution 2.20 Å R-free 0.238
4ZJJ PAK1 in complex with (S)-N-(tert-butyl)-3-((2-chloro-5-ethyl-8-fluoro-dibenzodiazepin-11-yl)amino)pyrrolidine-1-carboxamide Deposited 2015-04-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 249–545（297 aa）	Not recorded	4OR (S)-N-(tert-butyl)-3-((2-chloro-5-ethyl-8-fluoro-dibenzodiazepin-11-yl)amino)pyrrolidine-1-carboxamide × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；Equal volumes (0.8 uL) of reservoir solution and protein solution were mixed. Reservoir solution: 16.8% (w/v) PEG3350, 0.2 M magnesium formate (dihydrate)	Resolution 2.20 Å R-free 0.238
4ZJJ PAK1 in complex with (S)-N-(tert-butyl)-3-((2-chloro-5-ethyl-8-fluoro-dibenzodiazepin-11-yl)amino)pyrrolidine-1-carboxamide Deposited 2015-04-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 249–545（297 aa）	Not recorded	4OR (S)-N-(tert-butyl)-3-((2-chloro-5-ethyl-8-fluoro-dibenzodiazepin-11-yl)amino)pyrrolidine-1-carboxamide × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；Equal volumes (0.8 uL) of reservoir solution and protein solution were mixed. Reservoir solution: 16.8% (w/v) PEG3350, 0.2 M magnesium formate (dihydrate)	Resolution 2.20 Å R-free 0.238
4ZLO Serine/threonine-protein kinase PAK1 complexed with a dibenzodiazepine: identification of an allosteric site on PAK1 Deposited 2015-05-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 249–545（297 aa） Chain B 249–545（297 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	4PV 2,8-difluoro-11-(4-methylpiperazin-1-yl)-5H-dibenzo[b,e][1,4]diazepine × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；22-27% PEG3350, 500-700MM NACL, 100MM BIS-TRIS, PH 6.5	Resolution 2.50 Å R-free 0.222
4ZLO Serine/threonine-protein kinase PAK1 complexed with a dibenzodiazepine: identification of an allosteric site on PAK1 Deposited 2015-05-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 249–545（297 aa） Chain B 249–545（297 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	4PV 2,8-difluoro-11-(4-methylpiperazin-1-yl)-5H-dibenzo[b,e][1,4]diazepine × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；22-27% PEG3350, 500-700MM NACL, 100MM BIS-TRIS, PH 6.5	Resolution 2.50 Å R-free 0.222
4ZY4 Crystal structure of P21 activated kinase 1 in complex with an inhibitor compound 4 Deposited 2015-05-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa） Fragment：Protein kinase domain residue 249-545	Mutation：D389N	4T3 2-(4-aminopiperidin-1-yl)-N-(5-cyclopropyl-1H-pyrazol-3-yl)thieno[3,2-d]pyrimidin-4-amine × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；292 K；25% PEG 3500, 0.2M Ammonium Sulfate and 0.1M Tris pH 8	Resolution 2.60 Å R-free 0.248
4ZY4 Crystal structure of P21 activated kinase 1 in complex with an inhibitor compound 4 Deposited 2015-05-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 249–545（297 aa） Fragment：Protein kinase domain residue 249-545	Mutation：D389N	4T3 2-(4-aminopiperidin-1-yl)-N-(5-cyclopropyl-1H-pyrazol-3-yl)thieno[3,2-d]pyrimidin-4-amine × 1 DMS DIMETHYL SULFOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；292 K；25% PEG 3500, 0.2M Ammonium Sulfate and 0.1M Tris pH 8	Resolution 2.60 Å R-free 0.248
4ZY5 Crystal Structure of p21-activated kinase 1 in complex with an inhibitor compound 17 Deposited 2015-05-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa） Fragment：Protein kinase domain residue 249-545	Not recorded	4T5 N~2~-[(trans-4-aminocyclohexyl)methyl]-N~4~-(3-cyclopropyl-1H-pyrazol-5-yl)pyrimidine-2,4-diamine × 1 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；292 K；25% PEG 3500, 0.2M Ammonium Sulfate and 0.1M Tris pH 8	Resolution 2.35 Å R-free 0.230
4ZY5 Crystal Structure of p21-activated kinase 1 in complex with an inhibitor compound 17 Deposited 2015-05-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 249–545（297 aa） Fragment：Protein kinase domain residue 249-545	Not recorded	4T5 N~2~-[(trans-4-aminocyclohexyl)methyl]-N~4~-(3-cyclopropyl-1H-pyrazol-5-yl)pyrimidine-2,4-diamine × 1 DMS DIMETHYL SULFOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；292 K；25% PEG 3500, 0.2M Ammonium Sulfate and 0.1M Tris pH 8	Resolution 2.35 Å R-free 0.230
4ZY6 Crystal structure of P21-activated kinase 1 in complex with an inhibitor compound 29 Deposited 2015-05-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa） Fragment：Protein kinase domain residue 249-545	Mutation：D389N	4T6 N~2~-[(7-chloro-1H-benzimidazol-6-yl)methyl]-N~4~-(5-cyclopropyl-1H-pyrazol-3-yl)pyrimidine-2,4-diamine × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；292 K；25% PEG 3500, 0.2M Ammonium Sulfate and 0.1M Tris pH 8	Resolution 2.15 Å R-free 0.239
4ZY6 Crystal structure of P21-activated kinase 1 in complex with an inhibitor compound 29 Deposited 2015-05-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 249–545（297 aa） Fragment：Protein kinase domain residue 249-545	Mutation：D389N	4T6 N~2~-[(7-chloro-1H-benzimidazol-6-yl)methyl]-N~4~-(5-cyclopropyl-1H-pyrazol-3-yl)pyrimidine-2,4-diamine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；292 K；25% PEG 3500, 0.2M Ammonium Sulfate and 0.1M Tris pH 8	Resolution 2.15 Å R-free 0.239
5DEW Crystal structure of PAK1 in complex with an inhibitor compound 5 Deposited 2015-08-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa） Fragment：Protein kinase domain residue 249-545	Mutation：D389N, T423E	59N 8-[(trans-4-aminocyclohexyl)methyl]-6-[2-chloro-4-(6-methylpyrazin-2-yl)phenyl]-2-(ethylamino)pyrido[2,3-d]pyrimidin-7(8H)-one × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；292 K；crystals were grown at 19 C from 1.0 uL + 1.0 uL vapor diffusion drops containing 10 mg/mL protein, 1 mM ligand, 0.15 M DL-Malic Acid pH 7.0, 20% - 30% PEG 3350, 4% 1,3-Propanediol and 0.1 M Sodium Malonate, VAPOR DIFFUSION, SITTING DROP, temperature 292K	Resolution 1.90 Å R-free 0.215
5DEW Crystal structure of PAK1 in complex with an inhibitor compound 5 Deposited 2015-08-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 249–545（297 aa） Fragment：Protein kinase domain residue 249-545	Mutation：D389N, T423E	59N 8-[(trans-4-aminocyclohexyl)methyl]-6-[2-chloro-4-(6-methylpyrazin-2-yl)phenyl]-2-(ethylamino)pyrido[2,3-d]pyrimidin-7(8H)-one × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；292 K；crystals were grown at 19 C from 1.0 uL + 1.0 uL vapor diffusion drops containing 10 mg/mL protein, 1 mM ligand, 0.15 M DL-Malic Acid pH 7.0, 20% - 30% PEG 3350, 4% 1,3-Propanediol and 0.1 M Sodium Malonate, VAPOR DIFFUSION, SITTING DROP, temperature 292K	Resolution 1.90 Å R-free 0.215
5DEY Crystal structure of PAK1 in complex with an inhibitor compound G-5555 Deposited 2015-08-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa） Fragment：Protein kinase domain residue 249-545	Mutation：D389N, T423E	59T 8-[(trans-5-amino-1,3-dioxan-2-yl)methyl]-6-[2-chloro-4-(6-methylpyridin-2-yl)phenyl]-2-(methylamino)pyrido[2,3-d]pyrimidin-7(8H)-one × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；292 K；crystals were grown at 19 C from 1.0 uL + 1.0 uL vapor diffusion drops containing 10 mg/mL protein, 1 mM ligand, 0.15 M DL-Malic Acid pH 7.0, 20% - 30% PEG 3350, 4% 1,3-Propanediol and 0.1 M Sodium Malonate, VAPOR DIFFUSION, SITTING DROP, temperature 292K	Resolution 2.10 Å R-free 0.228
5DEY Crystal structure of PAK1 in complex with an inhibitor compound G-5555 Deposited 2015-08-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 249–545（297 aa） Fragment：Protein kinase domain residue 249-545	Mutation：D389N, T423E	59T 8-[(trans-5-amino-1,3-dioxan-2-yl)methyl]-6-[2-chloro-4-(6-methylpyridin-2-yl)phenyl]-2-(methylamino)pyrido[2,3-d]pyrimidin-7(8H)-one × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；292 K；crystals were grown at 19 C from 1.0 uL + 1.0 uL vapor diffusion drops containing 10 mg/mL protein, 1 mM ligand, 0.15 M DL-Malic Acid pH 7.0, 20% - 30% PEG 3350, 4% 1,3-Propanediol and 0.1 M Sodium Malonate, VAPOR DIFFUSION, SITTING DROP, temperature 292K	Resolution 2.10 Å R-free 0.228
5DFP Crystal structure of PAK1 in complex with an inhibitor compound FRAX1036 Deposited 2015-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa） Fragment：Protein kinase domain residue 249-545	Mutation：K299R Non-standard monomer：Yes (specific site not provided by mmCIF)	59U 6-[2-chloro-4-(6-methylpyrazin-2-yl)phenyl]-8-ethyl-2-{[2-(1-methylpiperidin-4-yl)ethyl]amino}pyrido[2,3-d]pyrimidin-7(8H)-one × 1 DMS DIMETHYL SULFOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；1 uL of PAK1 (9 mg/ml) with 1 uL of crystallization solution (0.1 M HEPES pH 7.0, 1 M NaCl, 25% PEG 3350, 10 mM DTT) at 4C	Resolution 2.20 Å R-free 0.246
5IME Crystal structure of P21-activated kinase 1 (PAK1) in complex with compound 9 Deposited 2016-03-06	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa） Fragment：residues 249-545	Not recorded	6BZ 8-(3-aminopropyl)-6-[2-chloro-4-(3-methyl-2-oxopyrazin-1(2H)-yl)phenyl]-2-(methylamino)pyrido[2,3-d]pyrimidin-7(8H)-one × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；292 K；crystals were grown at 19 C from 1.0 uL + 1.0 uL vapor diffusion drops containing 10 mg/mL protein, 1 mM ligand, 0.15 M DL-Malic Acid, 20% - 30% PEG 3350, 4% 1,3-Propanediol and 0.1 M Sodium Malonate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 292K	Resolution 2.22 Å R-free 0.263
5IME Crystal structure of P21-activated kinase 1 (PAK1) in complex with compound 9 Deposited 2016-03-06	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 249–545（297 aa） Fragment：residues 249-545	Not recorded	6BZ 8-(3-aminopropyl)-6-[2-chloro-4-(3-methyl-2-oxopyrazin-1(2H)-yl)phenyl]-2-(methylamino)pyrido[2,3-d]pyrimidin-7(8H)-one × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；292 K；crystals were grown at 19 C from 1.0 uL + 1.0 uL vapor diffusion drops containing 10 mg/mL protein, 1 mM ligand, 0.15 M DL-Malic Acid, 20% - 30% PEG 3350, 4% 1,3-Propanediol and 0.1 M Sodium Malonate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 292K	Resolution 2.22 Å R-free 0.263
5KBQ Pak1 in complex with bis-anilino pyrimidine inhibitor Deposited 2016-06-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 254–542（289 aa）	Mutation：D389N, T423E, E503D	IPV [4-methyl-3-[methyl-[2-[(3-methylsulfonyl-5-morpholin-4-yl-phenyl)amino]pyrimidin-4-yl]amino]phenyl]methanol × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.6；293 K；0.2M ammonium sulphate, 16% PEG 3350, 0.1M Hepes (pH 7.6)	Resolution 2.58 Å R-free 0.230
5KBQ Pak1 in complex with bis-anilino pyrimidine inhibitor Deposited 2016-06-03	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 254–542（289 aa）	Mutation：D389N, T423E, E503D	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.6；293 K；0.2M ammonium sulphate, 16% PEG 3350, 0.1M Hepes (pH 7.6)	Resolution 2.58 Å R-free 0.230
5KBR Pak1 in complex with 7-azaindole inhibitor Deposited 2016-06-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 254–542（289 aa）	Mutation：D389N, T423E, E503D	IPW (4-chlorophenyl)-[5-(1-piperidin-4-ylpyrazol-4-yl)-1~{H}-pyrrolo[2,3-b]pyridin-3-yl]methanone × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.6；293 K；0.2M ammonium sulphate, 16% PEG 3350, 0.1M Hepes (pH 7.6)	Resolution 2.36 Å R-free 0.255
5KBR Pak1 in complex with 7-azaindole inhibitor Deposited 2016-06-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 254–542（289 aa）	Mutation：D389N, T423E, E503D	IPW (4-chlorophenyl)-[5-(1-piperidin-4-ylpyrazol-4-yl)-1~{H}-pyrrolo[2,3-b]pyridin-3-yl]methanone × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.6；293 K；0.2M ammonium sulphate, 16% PEG 3350, 0.1M Hepes (pH 7.6)	Resolution 2.36 Å R-free 0.255
6B16 P21-activated kinase 1 in complex with a 4-azaindole inhibitor Deposited 2017-09-16	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa） Fragment：UNP residues 249-545	Not recorded	C7Y N~4~-(5-cyclopropyl-1H-pyrazol-3-yl)-N~2~-[(1S)-1-(1H-pyrrolo[3,2-b]pyridin-5-yl)ethyl]pyrimidine-2,4-diamine × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；292 K；25% PEG 3500, 0.2M Ammonium Sulfate and 0.1M Tris pH 8	Resolution 2.29 Å R-free 0.250
6B16 P21-activated kinase 1 in complex with a 4-azaindole inhibitor Deposited 2017-09-16	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 249–545（297 aa） Fragment：UNP residues 249-545	Not recorded	C7Y N~4~-(5-cyclopropyl-1H-pyrazol-3-yl)-N~2~-[(1S)-1-(1H-pyrrolo[3,2-b]pyridin-5-yl)ethyl]pyrimidine-2,4-diamine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；292 K；25% PEG 3500, 0.2M Ammonium Sulfate and 0.1M Tris pH 8	Resolution 2.29 Å R-free 0.250
7VTO The crystal structure of PAK1 with the inhibitor GW8510 Deposited 2021-10-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	107 4-[(7-OXO-7H-THIAZOLO[5,4-E]INDOL-8-YLMETHYL)-AMINO]-N-PYRIDIN-2-YL-BENZENESULFONAMIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；0.1 M Tris pH 8.5, 0.2 MgCl2, 24% PEG 3350, 5 mM TCEP	Resolution 2.59 Å R-free 0.252
7VTO The crystal structure of PAK1 with the inhibitor GW8510 Deposited 2021-10-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 249–545（297 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	107 4-[(7-OXO-7H-THIAZOLO[5,4-E]INDOL-8-YLMETHYL)-AMINO]-N-PYRIDIN-2-YL-BENZENESULFONAMIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；0.1 M Tris pH 8.5, 0.2 MgCl2, 24% PEG 3350, 5 mM TCEP	Resolution 2.59 Å R-free 0.252
8X5Z The Crystal Structure of PAK1 kinase domain from Biortus. Deposited 2023-11-20	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa）	Mutation：K299R,E503D Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1M SPG pH6.0, 25% PEG 1500	Resolution 1.80 Å R-free 0.216
9D4V Structure of PAK1 in complex with compound 7 Deposited 2024-08-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–476（228 aa） Chain A 477–545（69 aa）	Mutation：D389N,T423E Mutation：D389N,T423E	A1A2P N~2~-{[(1s,4s)-4-aminocyclohexyl]methyl}-N~4~-(5-cyclopropyl-1,3-thiazol-2-yl)pyrimidine-2,4-diamine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；0.2 M Na-malonate, pH 7.0, 0.15 M DL-malic acid, 4% propane-diol, and 16% PEG 3350	Resolution 1.84 Å R-free 0.269
9D4V Structure of PAK1 in complex with compound 7 Deposited 2024-08-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 249–476（228 aa） Chain B 477–545（69 aa）	Mutation：D389N,T423E Mutation：D389N,T423E	A1A2P N~2~-{[(1s,4s)-4-aminocyclohexyl]methyl}-N~4~-(5-cyclopropyl-1,3-thiazol-2-yl)pyrimidine-2,4-diamine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；0.2 M Na-malonate, pH 7.0, 0.15 M DL-malic acid, 4% propane-diol, and 16% PEG 3350	Resolution 1.84 Å R-free 0.269
9D4W Structure of PAK1 in complex with compound 12 Deposited 2024-08-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa）	Mutation：D389N, T423E	A1A2Q N~2~-{[(1s,4s)-4-aminocyclohexyl]methyl}-N~4~-[5-(trifluoromethyl)-1,3-thiazol-2-yl]pyrimidine-2,4-diamine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.6；293 K；0.1 M Na-malonate buffer, pH 6.6 , 0.15 M DL-malic acid, 4% propanediol, and 20% PEG 3350	Resolution 2.22 Å R-free 0.232
9D4W Structure of PAK1 in complex with compound 12 Deposited 2024-08-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 249–545（297 aa）	Mutation：D389N, T423E	A1A2Q N~2~-{[(1s,4s)-4-aminocyclohexyl]methyl}-N~4~-[5-(trifluoromethyl)-1,3-thiazol-2-yl]pyrimidine-2,4-diamine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.6；293 K；0.1 M Na-malonate buffer, pH 6.6 , 0.15 M DL-malic acid, 4% propanediol, and 20% PEG 3350	Resolution 2.22 Å R-free 0.232
9D4X Structure of PAK1 in complex with compound 16 Deposited 2024-08-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 250–545（296 aa）	Mutation：D389N, T423E	A1A2S N~2~-{[(1R,3R,4S)-4-amino-3-(3-chlorophenyl)cyclohexyl]methyl}-N~4~-(5-cyclopropyl-1,3-thiazol-2-yl)pyrimidine-2,4-diamine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；0.1 M Na-malonate buffer, pH 6.8 , 0.15 M DL-malic acid, 4% propanediol, and 20% PEG 3350	Resolution 1.85 Å R-free 0.227
9D4X Structure of PAK1 in complex with compound 16 Deposited 2024-08-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 250–545（296 aa）	Mutation：D389N, T423E	A1A2S N~2~-{[(1R,3R,4S)-4-amino-3-(3-chlorophenyl)cyclohexyl]methyl}-N~4~-(5-cyclopropyl-1,3-thiazol-2-yl)pyrimidine-2,4-diamine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；0.1 M Na-malonate buffer, pH 6.8 , 0.15 M DL-malic acid, 4% propanediol, and 20% PEG 3350	Resolution 1.85 Å R-free 0.227
9D4Y Structure of PAK1 in complex with compound 31 Deposited 2024-08-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 249–545（297 aa）	Mutation：D389N, T423E	A1A2S N~2~-{[(1R,3R,4S)-4-amino-3-(3-chlorophenyl)cyclohexyl]methyl}-N~4~-(5-cyclopropyl-1,3-thiazol-2-yl)pyrimidine-2,4-diamine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.6；293 K；100 mM malonate pH 6.6, 150 mM malic acid, 22% PEG 3350, 4% 1,2-propanediol	Resolution 1.85 Å R-free 0.227
9D4Y Structure of PAK1 in complex with compound 31 Deposited 2024-08-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 249–545（297 aa）	Mutation：D389N, T423E	A1A2S N~2~-{[(1R,3R,4S)-4-amino-3-(3-chlorophenyl)cyclohexyl]methyl}-N~4~-(5-cyclopropyl-1,3-thiazol-2-yl)pyrimidine-2,4-diamine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.6；293 K；100 mM malonate pH 6.6, 150 mM malic acid, 22% PEG 3350, 4% 1,2-propanediol	Resolution 1.85 Å R-free 0.227
9D50 Structure of PAK1 in complex with compound 24 Deposited 2024-08-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 250–545（296 aa）	Mutation：D389N, T423E	A1A2T 3-cyano-N-[3-({6-[(5-cyclopropyl-1,3-thiazol-2-yl)amino]pyrazin-2-yl}amino)bicyclo[1.1.1]pentan-1-yl]azetidine-3-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；100 mM malonate pH 6.6, 150 mM malic acid, 19% PEG 3350, 4% 1,2-propanediol	Resolution 1.90 Å R-free 0.230
9D50 Structure of PAK1 in complex with compound 24 Deposited 2024-08-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 250–545（296 aa）	Mutation：D389N, T423E	A1A2T 3-cyano-N-[3-({6-[(5-cyclopropyl-1,3-thiazol-2-yl)amino]pyrazin-2-yl}amino)bicyclo[1.1.1]pentan-1-yl]azetidine-3-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；100 mM malonate pH 6.6, 150 mM malic acid, 19% PEG 3350, 4% 1,2-propanediol	Resolution 1.90 Å R-free 0.230
9N48 Crystal structure of PAK1 bound to compound C1 Deposited 2025-02-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 249–545（297 aa） Chain B 249–545（297 aa）	Not recorded	A1BV1 (6M)-8-[2-(2-aminoethoxy)ethyl]-6-[2-chloro-3-fluoro-4-(2-oxopyrrolidin-1-yl)phenyl]-2-(ethylamino)pyrido[2,3-d]pyrimidin-7(8H)-one × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；291 K；0.2 M Lithium Sulfate, 0.1 M Tris pH8.5, 30% PEG4000	Resolution 1.85 Å R-free 0.216
9N4U Crystal structure of PAK1 bound to compound R1 Deposited 2025-02-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 249–545（297 aa） Chain B 249–545（297 aa）	Not recorded	A1BV8 (3M)-3-[(4P)-2-chloro-4-(6-methylpyridin-2-yl)phenyl]-1-{2-[2-(dimethylamino)ethoxy]ethyl}-1,6-naphthyridin-2(1H)-one × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.2M Lithium Sulfate, 0.1M Tris pH 8.5, 30% PEG4000	Resolution 1.77 Å R-free 0.203
9NBX Crystal structure of PAK1 bound to C2 Deposited 2025-02-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 249–545（297 aa） Chain B 249–545（297 aa）	Not recorded	A1BW5 (6M)-8-(3-aminopropyl)-6-(4-butoxy-2-methylphenyl)-2-(methylamino)pyrido[2,3-d]pyrimidin-7(8H)-one × 2 DMS DIMETHYL SULFOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.2M Lithium Sulfate, 0.1M Tris pH8.5, 30% PEG 4000	Resolution 2.15 Å R-free 0.265

40 other PDB entries and 69 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PAK1_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–22； UniProt 183–204

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1zsg
Deposition date deposition_date	2005-05-24
Structure title title	beta PIX-SH3 complexed with an atypical peptide from alpha-PAK
Keywords keywords	SH3-peptide complex, TRANSFERASE; TRANSFERASE
Experimental Method method	SOLUTION NMR

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	14.34 Å
Radius of gyration Rg (electron density) rg_electron	13.82 Å
Forward intensity I(0) i0	1336050000.00
Molecular weight molecular_weight	297300.0 kDa
Excluded volume excluded_volume	366370 Å³
Envelope volume envelope_volume	40081 Å³
Hydration-shell volume shell_volume	17975 Å³
Envelope diameter envelope_diameter	61.4 Å
Shell Rg shell_rg	25.37 Å
Envelope Rg envelope_rg	19.90 Å
Shape Rg shape_rg	13.72 Å
Total Rg total_rg	14.32 Å
Total atoms total_atoms	41100
Residues n_residues	2610
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	56.1 Å
Rg (real space) rg_real	14.38 Å
Rg uncertainty (real space) rg_real_error	0.56 Å
I(0) (real space) i0_real	1.3360e+09
I(0) uncertainty (real space) i0_real_error	1.6710e+07
Rg (reciprocal space) rg_reciprocal	14.37 Å
I(0) (reciprocal space) i0_reciprocal	1336000000.0000
Solution quality estimate total_estimate	0.7729
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	16.3 Å
Skewness Skewness skewness	0.512
Kurtosis Kurtosis kurtosis	0.246
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	389700.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.434; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.744; Smooth: 0.996

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Rho guanine nucleotide exchange factor 7
Molecular weight formula_weight	7499.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	41100

MTDNSNNQLVVRAKFNFQQTNEDELSFSKGDVIHVTRVEEGGWWEGTLNGRTGWFPSNYVREVKA

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	Serine/threonine-protein kinase PAK 1
Molecular weight formula_weight	2423.7 kDa
EC 编号 ec_number	2.7.1.37
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

DATPPPVIAPRPEHTKSVYTRS

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	1zsgA00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	30 — SH3 type barrels.
Homologous superfamily homologous superfamily	40 — SH3 Domains

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8. Citations (1)

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fit	/app/data/saxs_computation/zs/1zsg/1zsg.fit
pddf	/app/data/pr_computation/zs/1zsg/1zsg.pr.out
profile	/app/data/saxs_computation/zs/1zsg/1zsg.dat

beta PIX-SH3 complexed with an atypical peptide from alpha-PAK

1. Protein Identity and Related Structures Protein Identity & Related Structures

Rho guanine nucleotide exchange factor 7

State in the Current Structure

Other States of the Same Protein in the Database

Serine/threonine-protein kinase PAK 1

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)