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5WC2

Crystal Structure of ADP-bound human TRIP13

Functional Information from GO Data
ChainGOidnamespacecontents
A0001556biological_processoocyte maturation
A0001673cellular_componentmale germ cell nucleus
A0003712molecular_functiontranscription coregulator activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005694cellular_componentchromosome
A0006302biological_processdouble-strand break repair
A0006366biological_processtranscription by RNA polymerase II
A0007094biological_processmitotic spindle assembly checkpoint signaling
A0007130biological_processsynaptonemal complex assembly
A0007131biological_processreciprocal meiotic recombination
A0007141biological_processmale meiosis I
A0007144biological_processfemale meiosis I
A0007283biological_processspermatogenesis
A0007286biological_processspermatid development
A0016887molecular_functionATP hydrolysis activity
A0030154biological_processcell differentiation
A0042802molecular_functionidentical protein binding
A0048477biological_processoogenesis
A0051321biological_processmeiotic cell cycle
A0051598biological_processmeiotic recombination checkpoint signaling
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue ADP A 501
ChainResidue
ASER138
AILE330
AGLY385
AARG386
AARG389
AHOH615
AHOH663
AHOH687
AVAL140
ATYR141
AGLY182
ATHR183
AGLY184
ALYS185
ATHR186
ASER187

Functional Information from PROSITE/UniProt
site_idPS00674
Number of Residues20
DetailsAAA AAA-protein family signature. VvILtTSNitekIDvAFvdR
ChainResidueDetails
AVAL293-ARG312

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AGLY179

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
ChainResidueDetails
AMET1

222926

PDB entries from 2024-07-24

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