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5B5V

Structure of full-length MOB1b

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0019209molecular_functionkinase activator activity
A0019900molecular_functionkinase binding
A0030295molecular_functionprotein kinase activator activity
A0031952biological_processregulation of protein autophosphorylation
A0035329biological_processhippo signaling
A0043539molecular_functionprotein serine/threonine kinase activator activity
A0046872molecular_functionmetal ion binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0019209molecular_functionkinase activator activity
B0019900molecular_functionkinase binding
B0030295molecular_functionprotein kinase activator activity
B0031952biological_processregulation of protein autophosphorylation
B0035329biological_processhippo signaling
B0043539molecular_functionprotein serine/threonine kinase activator activity
B0046872molecular_functionmetal ion binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005730cellular_componentnucleolus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0019209molecular_functionkinase activator activity
C0019900molecular_functionkinase binding
C0030295molecular_functionprotein kinase activator activity
C0031952biological_processregulation of protein autophosphorylation
C0035329biological_processhippo signaling
C0043539molecular_functionprotein serine/threonine kinase activator activity
C0046872molecular_functionmetal ion binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005730cellular_componentnucleolus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0019209molecular_functionkinase activator activity
D0019900molecular_functionkinase binding
D0030295molecular_functionprotein kinase activator activity
D0031952biological_processregulation of protein autophosphorylation
D0035329biological_processhippo signaling
D0043539molecular_functionprotein serine/threonine kinase activator activity
D0046872molecular_functionmetal ion binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005730cellular_componentnucleolus
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0019209molecular_functionkinase activator activity
E0019900molecular_functionkinase binding
E0030295molecular_functionprotein kinase activator activity
E0031952biological_processregulation of protein autophosphorylation
E0035329biological_processhippo signaling
E0043539molecular_functionprotein serine/threonine kinase activator activity
E0046872molecular_functionmetal ion binding
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005730cellular_componentnucleolus
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0019209molecular_functionkinase activator activity
F0019900molecular_functionkinase binding
F0030295molecular_functionprotein kinase activator activity
F0031952biological_processregulation of protein autophosphorylation
F0035329biological_processhippo signaling
F0043539molecular_functionprotein serine/threonine kinase activator activity
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
ACYS79
ACYS84
AHIS161
AHIS166

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 302
ChainResidue
AARG154
AARG157
EGLY6

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS161
BHIS166
BCYS79
BCYS84

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN C 301
ChainResidue
CCYS79
CCYS84
CHIS161
CHIS166

site_idAC5
Number of Residues3
Detailsbinding site for residue CL C 302
ChainResidue
CARG154
CARG157
FGLY6

site_idAC6
Number of Residues5
Detailsbinding site for residue ZN D 301
ChainResidue
DCYS79
DCYS84
DALA111
DHIS161
DHIS166

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine; by STK4/MST1","evidences":[{"source":"UniProtKB","id":"Q7L9L4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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