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4YZM

Humanized Roco4 bound to LRRK2-In1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue 4K4 A 1301
ChainResidue
AILE1032
APRO1158
ALEU1161
AGLY1035
ALYS1055
AMET1105
AGLU1106
ALEU1107
AVAL1108
APRO1109
AGLY1111

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 1302
ChainResidue
AASP1154
AASP1177
ASER1181

site_idAC3
Number of Residues9
Detailsbinding site for residue 4K4 B 1301
ChainResidue
BVAL1040
BLYS1055
BGLU1106
BLEU1107
BVAL1108
BPRO1109
BGLY1111
BPRO1158
BLEU1161

site_idAC4
Number of Residues3
Detailsbinding site for residue MG B 1302
ChainResidue
BASP1154
BASP1177
BLEU1191

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGGFGLVHkGrlvkdksv..........VAIK
ChainResidueDetails
AILE1032-LYS1055

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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