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4Z2B

The structure of human PDE12 residues 161-609 in complex with GSK3036342A

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue SO4 A 701
ChainResidue
AGLU207
ALYS377
AARG431
ASER432
ATYR458
AEDO702
AHOH822
AHOH843
AHOH893

site_idAC2
Number of Residues7
Detailsbinding site for residue EDO A 702
ChainResidue
ALYS377
ASER433
AHIS456
ALEU457
ATYR458
ATRP459
ASO4701

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 703
ChainResidue
APHE177
APRO274
AGLY275
ACYS277
AASP280
ALYS337

site_idAC4
Number of Residues9
Detailsbinding site for residue TRS A 704
ChainResidue
AHIS281
ALYS412
AGLU416
ASER580
AGLU583
AHOH818
AHOH857
AHOH936
AHOH1037

site_idAC5
Number of Residues19
Detailsbinding site for residue 4LC A 705
ChainResidue
APRO208
AGLU209
ATYR307
ATHR310
ASER313
AGLU351
ATRP459
APRO461
AASN498
ASER499
ATHR500
ATHR503
APHE556
AMG706
AHOH842
AHOH844
AHOH920
AHOH973
AHOH1098

site_idAC6
Number of Residues6
Detailsbinding site for residue MG A 706
ChainResidue
AGLU351
AASP598
A4LC705
AHOH828
AHOH847
AHOH1038

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:Q96LI5
ChainResidueDetails
AASP496

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:26055709, ECO:0000269|Ref.16, ECO:0007744|PDB:4Z0V, ECO:0007744|PDB:4ZKF
ChainResidueDetails
AGLU351

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|Ref.16, ECO:0007744|PDB:4ZKF
ChainResidueDetails
AASP496
AASN498

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER217

224201

PDB entries from 2024-08-28

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