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3ZZW

Crystal structure of the kinase domain of ROR2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1751
ChainResidue
AHIS558
ATYR624
ALEU627

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1752
ChainResidue
AMET665
ATYR666
AARG706

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1753
ChainResidue
ASER697
AASN698
AGLN699

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 1751
ChainResidue
BHIS594
BALA597
BGLN598
BHIS743
BARG747

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1752
ChainResidue
BARG638
BGLU639
BVAL640

Functional Information from PROSITE/UniProt
site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. VVHkDLATRNVLV
ChainResidueDetails
AVAL611-VAL623

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP615
BASP615

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU479
ALYS507
BLEU479
BLYS507

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Sulfoserine; partial => ECO:0000269|PubMed:14752058
ChainResidueDetails
ASER469
ASER471
BSER469
BSER471

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250
ChainResidueDetails
ATYR646
BTYR646

218853

PDB entries from 2024-04-24

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