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3FZP

Crystal structure of PYK2 complexed with ATPgS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AGS A 999
ChainResidue
AHOH16
ALEU504
ATYR505
AGLU509
ALEU556
APHE568
AGLY434
APHE435
APHE436
AVAL439
AALA455
ALYS457
AGLU474
AGLU503

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 2
ChainResidue
AHOH11
AHOH36
ALYS623
AASP648

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 3
ChainResidue
AHOH6
AHOH83
AHIS483
ALYS535

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGFFGEVYeGvytnhkgekin.......VAVK
ChainResidueDetails
ALEU431-LYS457

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CVHrDIAVRNILV
ChainResidueDetails
ACYS545-VAL557

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:PRU10028
ChainResidueDetails
AASP549

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:19244237, ECO:0007744|PDB:3FZP
ChainResidueDetails
ALEU431
ALYS457
AGLU503

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9QVP9
ChainResidueDetails
ATYR579

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by SRC, FYN and LCK => ECO:0000269|PubMed:20028775, ECO:0000269|PubMed:20381867
ChainResidueDetails
ATYR580

218853

PDB entries from 2024-04-24

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