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5AV1

Crystal structure of DAPK1 in the presence of bromide ions.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue BR A 301
ChainResidue
ALYS42
AASP161
ABR305

site_idAC2
Number of Residues4
Detailsbinding site for residue BR A 302
ChainResidue
AGLU17
ALYS29
AHOH426
AHOH642

site_idAC3
Number of Residues4
Detailsbinding site for residue BR A 303
ChainResidue
AHOH620
AHOH654
AHIS131
AILE266

site_idAC4
Number of Residues2
Detailsbinding site for residue BR A 304
ChainResidue
AGLN267
AHOH548

site_idAC5
Number of Residues4
Detailsbinding site for residue BR A 305
ChainResidue
ALEU93
AASP161
ABR301
AHOH520

site_idAC6
Number of Residues2
Detailsbinding site for residue BR A 306
ChainResidue
ALYS222
AARG254

site_idAC7
Number of Residues4
Detailsbinding site for residue BR A 307
ChainResidue
ALYS222
ATHR225
AHOH537
AHOH619

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues28
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGQFAVVKkCrekstglqyaak......FIKK
ChainResidueDetails
ALEU19-LYS46

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHfDLKpeNIML
ChainResidueDetails
AILE135-LEU147

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP139

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
ALEU19
ALYS42
AGLU94
AGLU100
AASP161

223166

PDB entries from 2024-07-31

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