4ejq

Crystal structure of KIF1A C-CC1-FHA

Method: X-RAY DIFFRACTION D_max: 127.3 Å Quality: GOOD

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

Kinesin-like protein KIF1A

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 458–607 Chain B； UniProt 458–607	Fragment：C-CC1-FHA, UNP residues 458-607	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.2；289 K；0.2 M calcium acetate hydrate, 18% (w/v) PEG 3000, 0.1 M Bis-Tris, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 1.89 Å R-free 0.231
2	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 458–607 Chain D； UniProt 458–607	Fragment：C-CC1-FHA, UNP residues 458-607	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.2；289 K；0.2 M calcium acetate hydrate, 18% (w/v) PEG 3000, 0.1 M Bis-Tris, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 1.89 Å R-free 0.231
3	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain E； UniProt 458–607 Chain F； UniProt 458–607	Fragment：C-CC1-FHA, UNP residues 458-607	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.2；289 K；0.2 M calcium acetate hydrate, 18% (w/v) PEG 3000, 0.1 M Bis-Tris, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 1.89 Å R-free 0.231
4	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain G； UniProt 458–607 Chain H； UniProt 458–607	Fragment：C-CC1-FHA, UNP residues 458-607	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.2；289 K；0.2 M calcium acetate hydrate, 18% (w/v) PEG 3000, 0.1 M Bis-Tris, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 1.89 Å R-free 0.231

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 4EJQ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4EGX Crystal structure of KIF1A CC1-FHA tandem Deposited 2012-04-02	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 430–607（178 aa） Fragment：CC1-FHA tandem, UNP residues 430-607 Chain B 430–607（178 aa） Fragment：CC1-FHA tandem, UNP residues 430-607	Not recorded	PEG DI(HYDROXYETHYL)ETHER × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；289 K；18% (w/v) PEG 5000 MME, 8% (v/v) Tacsimate (pH 6.0), 0.1 M Bis-Tris, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 2.51 Å R-free 0.283
4EGX Crystal structure of KIF1A CC1-FHA tandem Deposited 2012-04-02	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 430–607（178 aa） Fragment：CC1-FHA tandem, UNP residues 430-607 Chain D 430–607（178 aa） Fragment：CC1-FHA tandem, UNP residues 430-607	Not recorded	PEG DI(HYDROXYETHYL)ETHER × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；289 K；18% (w/v) PEG 5000 MME, 8% (v/v) Tacsimate (pH 6.0), 0.1 M Bis-Tris, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 2.51 Å R-free 0.283
4UXO Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins Deposited 2014-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 1–361（361 aa）	Not recorded	ZN ZINC ION × 1 MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1	ELECTRON MICROSCOPY cryo-EM buffer 20MM PIPES, 2MM MGCL2, 1MM EGTA, 2MM DTT, 10 U/ML APYRASE；pH 6.8；20MM PIPES, 2MM MGCL2, 1MM EGTA, 2MM DTT, 10 U/ML APYRASE cryo-EM vitrification conditions Cryogen ETHANE；LIQUID ETHANE	Resolution 6.30 Å
4UXP Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins Deposited 2014-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 1–361（361 aa）	Not recorded	ZN ZINC ION × 1 MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1	ELECTRON MICROSCOPY cryo-EM buffer 20MM PIPES, 2MM MGCL2, 1MM EGTA, 2MM DTT, 10 U/ML APYRASE；pH 6.8；20MM PIPES, 2MM MGCL2, 1MM EGTA, 2MM DTT, 10 U/ML APYRASE cryo-EM vitrification conditions Cryogen ETHANE；LIQUID ETHANE	Resolution 6.30 Å
4UXR Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins Deposited 2014-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 1–361（361 aa）	Not recorded	ZN ZINC ION × 1 MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ALF TETRAFLUOROALUMINATE ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.00 Å
4UXS Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins Deposited 2014-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 1–361（361 aa）	Not recorded	ZN ZINC ION × 1 MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1	ELECTRON MICROSCOPY cryo-EM buffer 20MM PIPES, 2MM MGCL2, 1MM EGTA, 2MM DTT, 2MM ADP；pH 6.8；20MM PIPES, 2MM MGCL2, 1MM EGTA, 2MM DTT, 2MM ADP cryo-EM vitrification conditions Cryogen ETHANE；LIQUID ETHANE	Resolution 7.00 Å
8UTN KIF1A[1-393] AMP-PNP bound two-heads-bound state in complex with a microtubule (class T23L1) Deposited 2023-10-31	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain K 1–393（393 aa） Fragment：residues 1-393 Chain N 1–393（393 aa） Fragment：residues 1-393	Not recorded	MG MAGNESIUM ION × 4 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 3 GDP GUANOSINE-5'-DIPHOSPHATE × 2 TA1 TAXOL × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
8UTO KIF1A[1-393] AMP-PNP bound two-heads-bound state in complex with a microtubule - class T2L1 Deposited 2023-10-31	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain K 1–393（393 aa） Fragment：residues 1-393 Chain N 1–393（393 aa） Fragment：residues 1-393	Not recorded	MG MAGNESIUM ION × 4 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 3 GDP GUANOSINE-5'-DIPHOSPHATE × 2 TA1 TAXOL × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8UTP KIF1A[1-393] - AMP-PNP two-heads-bound state in complex with a microtubule - class T3L1 Deposited 2023-10-31	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain K 1–393（393 aa） Fragment：residues 1-393 Chain N 1–393（393 aa） Fragment：residues 1-393	Not recorded	MG MAGNESIUM ION × 4 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 3 GDP GUANOSINE-5'-DIPHOSPHATE × 2 TA1 TAXOL × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8UTQ KIF1A[1-393] AMP-PNP bound one-head-bound state in complex with a microtubule - class T1L02* Deposited 2023-10-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain K 1–393（393 aa） Fragment：residues 1-393	Not recorded	MG MAGNESIUM ION × 3 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 TA1 TAXOL × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
8UTR KIF1A[1-393] ADP bound in complex with a microtubule Deposited 2023-10-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain K 1–393（393 aa） Fragment：residues 1-393	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
8UTS KIF1A[1-393] APO in complex with a microtubule Deposited 2023-10-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain K 1–393（393 aa） Fragment：residues 1-393	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.70 Å
8UTT KIF1A[1-393] P305L mutant AMP-PNP bound two-heads-bound state in complex with a microtubule Deposited 2023-10-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain K 1–393（393 aa） Fragment：residues 1-393 Chain N 1–393（393 aa） Fragment：residues 1-393	Mutation：P305L Mutation：P305L	MG MAGNESIUM ION × 4 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 3 GDP GUANOSINE-5'-DIPHOSPHATE × 2 TA1 TAXOL × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
8UTU KIF1A[1-393] P305L mutant AMP-PNP bound one and two heads bound states merged, in complex with a microtubule Deposited 2023-10-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain K 1–393（393 aa） Fragment：residues 1-393	Mutation：P305L	MG MAGNESIUM ION × 3 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
8UTV KIF1A[1-393] P305L mutant ADP bound in complex with a microtubule Deposited 2023-10-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain K 1–393（393 aa） Fragment：residues 1-393	Mutation：P305L	GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
8UTW KIF1A[1-393] P305L mutant APO in complex with a microtubule Deposited 2023-10-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain K 1–393（393 aa） Fragment：residues 1-393	Mutation：P305L	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
8UTY KIF1A[1-393] P364L mutant AMP-PNP bound two-heads-bound state in complex with a microtubule Deposited 2023-10-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain K 1–393（393 aa） Fragment：residues 1-393 Chain N 1–393（393 aa） Fragment：residues 1-393	Mutation：P364L Mutation：P364L	GTP GUANOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 GDP GUANOSINE-5'-DIPHOSPHATE × 2 TA1 TAXOL × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
9YA5 KIF1A R350G bound to microtubules in two-heads-bound state with AMP-PNP Deposited 2025-09-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain K 1–393（393 aa） Chain N 1–393（393 aa）	Mutation：R350G Mutation：R350G	GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 3 GDP GUANOSINE-5'-DIPHOSPHATE × 2 TA1 TAXOL × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8；BRB80 buffer composed of 80 mM PIPES, 2 mM MgCl2, 1 mM EGTA, PH 6.8 cryo-EM vitrification conditions Cryogen ETHANE；4uL of a 6uM MT solution in BRB80 (80mM PIPES, 2mM MgCl2, 1mM EGTA pH 6.8) along with 20uM paclitaxel was added onto a plasma-cleaned grid. The MTs were incubated for 1 minute at room temperature, and then the excess liquid was removed from the grid using Whatman #1 paper. Next, 4uL of a solution containing 20uM KIF1A-R350G in BRB80 supplemented with 20uM paclitaxel and 5mM AMP-PNP was added to the grid. The grid with the MT and kinesin mixture was then mounted into a Vitrobot, incubated for 1 minute at room temperature, and plunge-frozen into liquid nitrogen-cooled ethane.	Resolution 2.95 Å
9YA7 KIF1A R350G bound to microtubules in the apo state Deposited 2025-09-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain K 1–393（393 aa）	Mutation：R350	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8；BRB80 buffer composed of 80 mM PIPES, 2 mM MgCl2, 1 mM EGTA, PH 6.8 cryo-EM vitrification conditions Cryogen ETHANE；4uL of a 6uM MT solution in BRB80 (80mM PIPES, 2mM MgCl2, 1mM EGTA pH 6.8) along with 20uM paclitaxel was added onto a plasma-cleaned grid. The MTs were incubated for 1 minute at room temperature, and then the excess liquid was removed from the grid using Whatman #1 paper. Next, 4uL of a solution containing 20uM KIF1A-R350G in BRB80 supplemented with 20uM paclitaxel and 0.005 units per uL apyrase was added to the grid. The grid with the MT and kinesin mixture was then mounted into a Vitrobot, incubated for 1 minute at room temperature, and plunge-frozen into liquid nitrogen-cooled ethane.	Resolution 3.29 Å
9YAB KIF1A R350W bound to microtubules in the apo state Deposited 2025-09-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain K 1–393（393 aa）	Mutation：R350W	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8；BRB80 buffer composed of 80 mM PIPES, 2 mM MgCl2, 1 mM EGTA, PH 6.8 cryo-EM vitrification conditions Cryogen ETHANE；4uL of a 6uM MT solution in BRB80 (80mM PIPES, 2mM MgCl2, 1mM EGTA pH 6.8) along with 20uM paclitaxel was added onto a plasma-cleaned grid. The MTs were incubated for 1 minute at room temperature, and then the excess liquid was removed from the grid using Whatman #1 paper. Next, 4uL of a solution containing 17.5uM KIF1A-R350W in BRB80 supplemented with 20uM paclitaxel and 0.005 units per uL apyrase was added to the grid. The grid with the MT and kinesin mixture was then mounted into a Vitrobot, incubated for 1 minute at room temperature, and plunge-frozen into liquid nitrogen-cooled ethane.	Resolution 3.21 Å
9YAI KIF1A R350W bound to microtubules in two-heads-bound state with AMP-PNP Deposited 2025-09-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain K 1–393（393 aa） Chain N 1–393（393 aa）	Mutation：R350W Mutation：R350W	MG MAGNESIUM ION × 3 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 TA1 TAXOL × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8；BRB80 buffer composed of 80 mM PIPES, 2 mM MgCl2, 1 mM EGTA, PH 6.8 cryo-EM vitrification conditions Cryogen ETHANE；4uL of a 6uM MT solution in BRB80 (80mM PIPES, 2mM MgCl2, 1mM EGTA pH 6.8) along with 20uM paclitaxel was added onto a plasma-cleaned grid. The MTs were incubated for 1 minute at room temperature, and then the excess liquid was removed from the grid using Whatman #1 paper. Next, 4uL of a solution containing 17.5uM KIF1A-R350W in BRB80 supplemented with 20uM paclitaxel and 5mM AMP-PNP was added to the grid. The grid with the MT and kinesin mixture was then mounted into a Vitrobot, incubated for 1 minute at room temperature, and plunge-frozen into liquid nitrogen-cooled ethane.	Resolution 3.12 Å

20 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	KIF1A_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–154； UniProt 458–607 Author chain B； PDBConstruct 5–154； UniProt 458–607 Author chain C； PDBConstruct 5–154； UniProt 458–607 Author chain D； PDBConstruct 5–154； UniProt 458–607 Author chain E； PDBConstruct 5–154； UniProt 458–607 Author chain F； PDBConstruct 5–154； UniProt 458–607 Author chain G； PDBConstruct 5–154； UniProt 458–607 Author chain H； PDBConstruct 5–154； UniProt 458–607

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	4ejq
Deposition date deposition_date	2012-04-06
Structure title title	Crystal structure of KIF1A C-CC1-FHA
Keywords keywords	HOMODIMER, FHA DOMAIN, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	40.75 Å
Radius of gyration Rg (electron density) rg_electron	40.43 Å
Forward intensity I(0) i0	300846000.00
Molecular weight molecular_weight	134120.0 kDa
Excluded volume excluded_volume	165270 Å³
Envelope volume envelope_volume	240610 Å³
Hydration-shell volume shell_volume	51067 Å³
Envelope diameter envelope_diameter	131.9 Å
Shell Rg shell_rg	44.37 Å
Envelope Rg envelope_rg	39.59 Å
Shape Rg shape_rg	40.43 Å
Total Rg total_rg	40.62 Å
Total atoms total_atoms	9396
Residues n_residues	1194
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	127.3 Å
Rg (real space) rg_real	40.77 Å
Rg uncertainty (real space) rg_real_error	1.01 Å
I(0) (real space) i0_real	3.0080e+08
I(0) uncertainty (real space) i0_real_error	5.0460e+06
Rg (reciprocal space) rg_reciprocal	40.75 Å
I(0) (reciprocal space) i0_reciprocal	300800000.0000
Solution quality estimate total_estimate	0.8768
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	39.2 Å
Skewness Skewness skewness	0.260
Kurtosis Kurtosis kurtosis	-0.702
Angular range angular_range	— – 0.1950 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	35640000.0000
Real-space data points n_real_points	40
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.959; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.972; Smooth: 0.547

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 16 domains

CATH v4.4 (16 domains)

Domain ID domain_id	4ejqA01
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	2530 —

Domain ID domain_id	4ejqA02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	200 — Tumour Suppressor Smad4
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	4ejqB01
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	2530 —

Domain ID domain_id	4ejqB02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	200 — Tumour Suppressor Smad4
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	4ejqC01
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	2530 —

Domain ID domain_id	4ejqC02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	200 — Tumour Suppressor Smad4
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	4ejqD01
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	2530 —

Domain ID domain_id	4ejqD02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	200 — Tumour Suppressor Smad4
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	4ejqE01
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	2530 —

Domain ID domain_id	4ejqE02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	200 — Tumour Suppressor Smad4
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	4ejqF01
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	2530 —

Domain ID domain_id	4ejqF02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	200 — Tumour Suppressor Smad4
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	4ejqG01
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	2530 —

Domain ID domain_id	4ejqG02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	200 — Tumour Suppressor Smad4
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	4ejqH01
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	2530 —

Domain ID domain_id	4ejqH02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	200 — Tumour Suppressor Smad4
Homologous superfamily homologous superfamily	20 —

▶

8. Citations (1)

▶

Unit-cell length a length_a	42.945 Å
Unit-cell length b length_b	57.844 Å
Unit-cell length c length_c	110.394 Å
Unit-cell angle α angle_alpha	89.98 °
Unit-cell angle β angle_beta	89.96 °
Unit-cell angle γ angle_gamma	90.63 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	1.893 Å
Low-resolution limit resolution_low	33.906 Å
R factor r_factor	0.1883
R_work r_work	0.1872
R_free r_free	0.2313

Description description	Kinesin-like protein KIF1A
Molecular weight formula_weight	17378.6 kDa
Source method src_method	man
Copy count entity_count	8

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H
Atom count atom_count	10054

Crystal structure of KIF1A C-CC1-FHA

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

Kinesin-like protein KIF1A

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

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 16 domains

CATH v4.4 (16 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

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

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	658

fit	/app/data/saxs_computation/ej/4ejq/4ejq.fit
pddf	/app/data/pr_computation/ej/4ejq/4ejq.pr.out
profile	/app/data/saxs_computation/ej/4ejq/4ejq.dat