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5KMG

Near-atomic cryo-EM structure of PRC1 bound to the microtubule

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000226biological_processmicrotubule cytoskeleton organization
A0000278biological_processmitotic cell cycle
A0003924molecular_functionGTPase activity
A0005200molecular_functionstructural constituent of cytoskeleton
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0007017biological_processmicrotubule-based process
A0015630cellular_componentmicrotubule cytoskeleton
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000226biological_processmicrotubule cytoskeleton organization
B0000278biological_processmitotic cell cycle
B0001764biological_processneuron migration
B0003924molecular_functionGTPase activity
B0005200molecular_functionstructural constituent of cytoskeleton
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0007017biological_processmicrotubule-based process
B0046872molecular_functionmetal ion binding
P0000226biological_processmicrotubule cytoskeleton organization
P0008017molecular_functionmicrotubule binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue GTP A 501
ChainResidue
AGLY10
AGLY144
ATHR145
AGLY146
ATHR179
AASN206
ATYR224
AASN228
AMG502
BLYS254
AGLN11
AALA12
AGLN15
AASP98
AALA99
AASN101
ASER140
AGLY143

site_idAC2
Number of Residues1
Detailsbinding site for residue MG A 502
ChainResidue
AGTP501

site_idAC3
Number of Residues14
Detailsbinding site for residue GDP B 501
ChainResidue
BGLY10
BGLN11
BCYS12
BGLN15
BASN101
BSER140
BGLY143
BGLY144
BTHR145
BGLY146
BASP179
BASN206
BTYR224
BASN228

site_idAC4
Number of Residues7
Detailsbinding site for residue POU B 502
ChainResidue
BPHE296
BASP297
BALA298
BARG308
BTYR312
BVAL335
BTYR342

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Tubulin binding
ChainResidueDetails
PARG377
PLYS387
BGLY144
BTHR145
BGLY146
BASN206
BASN228

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
BGLU71
AGLU71
ASER140
AGLY144
ATHR145
ATHR179
AASN206
AASN228

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P99024
ChainResidueDetails
BSER40

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024
ChainResidueDetails
BLYS60
ASER232

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885
ChainResidueDetails
BSER174

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BTHR287
BTHR292

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BARG320

site_idSWS_FT_FI8
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BLYS60
ALYS370

site_idSWS_FT_FI9
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BLYS326

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PDB entries from 2025-06-11

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