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1VFW

Crystal Structure of the Kif1A Motor Domain Complexed With Mg-AMPPNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003777molecular_functionmicrotubule motor activity
A0005524molecular_functionATP binding
A0007018biological_processmicrotubule-based movement
A0008017molecular_functionmicrotubule binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
ASER104
AANP500
AHOH513

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ANP A 500
ChainResidue
ATYR67
ATHR99
AGLY100
AALA101
AGLY102
ALYS103
ASER104
ATYR105
ALYS110
ASER214
ASER215
AGLY251
AMG501
AHOH503
AHOH523
AHOH544
AARG11
AARG13
APRO14
AGLU63
AASP64
AILE65

Functional Information from PROSITE/UniProt
site_idPS00411
Number of Residues12
DetailsKINESIN_MOTOR_1 Kinesin motor domain signature. SKIsLVDLAGSE
ChainResidueDetails
ASER242-GLU253

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18806800, ECO:0000269|PubMed:35132656, ECO:0000305|PubMed:15286375, ECO:0007744|PDB:1VFX, ECO:0007744|PDB:1VFZ, ECO:0007744|PDB:2ZFI, ECO:0007744|PDB:2ZFJ, ECO:0007744|PDB:2ZFK, ECO:0007744|PDB:2ZFL, ECO:0007744|PDB:2ZFM, ECO:0007744|PDB:7EO9, ECO:0007744|PDB:7EOB
ChainResidueDetails
ATYR67

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18806800, ECO:0000269|PubMed:35132656, ECO:0000305|PubMed:15286375, ECO:0007744|PDB:1VFX, ECO:0007744|PDB:1VFZ, ECO:0007744|PDB:2ZFI, ECO:0007744|PDB:2ZFK, ECO:0007744|PDB:2ZFL, ECO:0007744|PDB:2ZFM, ECO:0007744|PDB:7EO9, ECO:0007744|PDB:7EOB
ChainResidueDetails
AGLY100

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18806800, ECO:0000269|PubMed:35132656, ECO:0000305|PubMed:15286375, ECO:0007744|PDB:1VFX, ECO:0007744|PDB:2ZFJ, ECO:0007744|PDB:2ZFK, ECO:0007744|PDB:2ZFL, ECO:0007744|PDB:2ZFM, ECO:0007744|PDB:7EO9
ChainResidueDetails
AALA101

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:15286375, ECO:0007744|PDB:1VFV, ECO:0007744|PDB:1VFW
ChainResidueDetails
AGLY102
ALYS103
ATYR105
ASER215

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15286375, ECO:0000269|PubMed:18806800, ECO:0000269|PubMed:35132656, ECO:0007744|PDB:1VFV, ECO:0007744|PDB:1VFW, ECO:0007744|PDB:1VFX, ECO:0007744|PDB:1VFZ, ECO:0007744|PDB:2ZFI, ECO:0007744|PDB:2ZFK, ECO:0007744|PDB:7EO9, ECO:0007744|PDB:7EOB
ChainResidueDetails
ASER104

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1goj
ChainResidueDetails
AGLY251

237423

PDB entries from 2025-06-11

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