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2P4N

Human Monomeric Kinesin (1BG2) and Bovine Tubulin (1JFF) Docked into the 9-Angstrom Cryo-EM Map of Nucleotide-Free Kinesin Complexed to the Microtubule

Functional Information from GO Data
ChainGOidnamespacecontents
A0000226biological_processmicrotubule cytoskeleton organization
A0000278biological_processmitotic cell cycle
A0005200molecular_functionstructural constituent of cytoskeleton
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0007017biological_processmicrotubule-based process
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0000226biological_processmicrotubule cytoskeleton organization
B0000278biological_processmitotic cell cycle
B0003924molecular_functionGTPase activity
B0005200molecular_functionstructural constituent of cytoskeleton
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0007017biological_processmicrotubule-based process
B0007399biological_processnervous system development
B0015630cellular_componentmicrotubule cytoskeleton
B0046872molecular_functionmetal ion binding
B0046982molecular_functionprotein heterodimerization activity
B1902669biological_processpositive regulation of axon guidance
K0003777molecular_functionmicrotubule motor activity
K0005524molecular_functionATP binding
K0007018biological_processmicrotubule-based movement
K0008017molecular_functionmicrotubule binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG K 402
ChainResidue
KTHR92
KADP401

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ZN A 900
ChainResidue
AHIS283

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
AGLN11
AGLU71
BGTP500

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ADP K 401
ChainResidue
KGLN86
KTHR87
KSER88
KSER89
KGLY90
KLYS91
KTHR92
KHIS93
KMG402
KARG14
KARG16
KPRO17

site_idAC5
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GTP B 500
ChainResidue
AGLY10
AGLN11
AALA12
AGLN15
AALA99
AALA100
AASN101
ASER140
AGLY143
AGLY144
ATHR145
AGLY146
AILE171
AGLU183
AASN206
ATYR224
AASN228
AMG501
BLEU248
BLYS254

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GDP B 600
ChainResidue
BGLY10
BGLN11
BCYS12
BGLN15
BSER140
BGLY142
BGLY144
BTHR145
BGLY146
BASP179
BASN206
BTYR224
BASN228

site_idAC7
Number of Residues15
DetailsBINDING SITE FOR RESIDUE TA1 B 601
ChainResidue
BVAL23
BASP26
BGLU27
BHIS229
BLEU230
BALA233
BSER236
BPHE272
BPRO274
BLEU275
BTHR276
BARG278
BPRO360
BARG369
BGLY370

Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
ChainResidueDetails
BGLY142-GLY148
AGLY142-GLY148

site_idPS00228
Number of Residues4
DetailsTUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI
ChainResidueDetails
BMET1-ILE4

site_idPS00411
Number of Residues12
DetailsKINESIN_MOTOR_1 Kinesin motor domain signature. GKLyLVDLAGSE
ChainResidueDetails
KGLY225-GLU236

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING:
ChainResidueDetails
KGLY85
BSER140
BGLY144
BTHR145
BGLY146
BASN206
BASN228

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
KALA2
AGLU71
ASER140
AGLY144
ATHR145
ATHR179
AASN206
AASN228

site_idSWS_FT_FI3
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
KLYS213

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8
ChainResidueDetails
BALA57

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024
ChainResidueDetails
BLYS60

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1
ChainResidueDetails
BSER174

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BTHR287
BTHR292

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BARG320

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:Q2T9S0
ChainResidueDetails
BGLU448

site_idSWS_FT_FI10
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BLYS60

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BLYS326

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1goj
ChainResidueDetails
KGLY234

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PDB entries from 2024-07-17

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