Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4OZQ

Crystal structure of the mouse Kif14 motor domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0003777molecular_functionmicrotubule motor activity
A0005524molecular_functionATP binding
A0007018biological_processmicrotubule-based movement
A0008017molecular_functionmicrotubule binding
A0008643biological_processcarbohydrate transport
A0015144molecular_functioncarbohydrate transmembrane transporter activity
A0055085biological_processtransmembrane transport
B0003777molecular_functionmicrotubule motor activity
B0005524molecular_functionATP binding
B0007018biological_processmicrotubule-based movement
B0008017molecular_functionmicrotubule binding
B0008643biological_processcarbohydrate transport
B0015144molecular_functioncarbohydrate transmembrane transporter activity
B0055085biological_processtransmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue ADP A 801
ChainResidue
AARG399
ASER489
ATYR490
AHOH905
AARG401
APRO402
ASER444
AGLN483
AGLY485
ASER486
AGLY487
ALYS488

site_idAC2
Number of Residues7
Detailsbinding site for residue EDO A 802
ChainResidue
AVAL532
AASN534
AGLU535
ASER660
AILE661
ASER664
AHOH912

site_idAC3
Number of Residues14
Detailsbinding site for residue ADP B 801
ChainResidue
BARG399
BARG401
BPRO402
BSER444
BGLN483
BTHR484
BGLY485
BSER486
BGLY487
BLYS488
BSER489
BTYR490
BHOH913
BHOH919

site_idAC4
Number of Residues6
Detailsbinding site for residue EDO B 802
ChainResidue
BVAL532
BASN534
BGLU535
BSER660
BILE661
BSER664

Functional Information from PROSITE/UniProt
site_idPS00411
Number of Residues12
DetailsKINESIN_MOTOR_1 Kinesin motor domain signature. SRInLVDLAGSE
ChainResidueDetails
ASER632-GLU643

site_idPS01037
Number of Residues18
DetailsSBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN
ChainResidueDetails
APRO-263-ASN-246

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00283, ECO:0007744|PDB:4OZQ
ChainResidueDetails
AGLY482
BGLY482

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon