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6F8V

Crystal structure of the PDE4D catalytic domain in complex with GEBR-18b

Functional Information from GO Data
ChainGOidnamespacecontents
A0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
A0007165biological_processsignal transduction
A0008081molecular_functionphosphoric diester hydrolase activity
B0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
B0007165biological_processsignal transduction
B0008081molecular_functionphosphoric diester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue ZN A 601
ChainResidue
AHIS330
AHIS366
AASP367
AASP484
AHOH731
AHOH814

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 602
ChainResidue
AHOH803
AHOH817
AHOH906
AASP367
AHOH731
AHOH748

site_idAC3
Number of Residues3
Detailsbinding site for residue MG A 603
ChainResidue
AASP264
AHOH710
AHOH798

site_idAC4
Number of Residues6
Detailsbinding site for residue MG A 604
ChainResidue
AASP467
AASP471
AHIS527
AHOH800
AHOH809
AHOH820

site_idAC5
Number of Residues14
Detailsbinding site for residue D0B A 605
ChainResidue
ATYR325
ATHR437
AMET439
AASP484
ALEU485
AASN487
AILE502
APHE506
AMET523
AGLN535
APHE538
AHOH737
AHOH834
AHOH873

site_idAC6
Number of Residues6
Detailsbinding site for residue ZN B 601
ChainResidue
BHIS330
BHIS366
BASP367
BASP484
BHOH712
BHOH753

site_idAC7
Number of Residues6
Detailsbinding site for residue MG B 602
ChainResidue
BASP367
BHOH712
BHOH751
BHOH779
BHOH801
BHOH807

site_idAC8
Number of Residues13
Detailsbinding site for residue D0B B 603
ChainResidue
BTHR437
BMET439
BASP484
BLEU485
BASN487
BTHR499
BILE502
BPHE506
BMET523
BGLN535
BPHE538
BHOH787
BHOH812

Functional Information from PROSITE/UniProt
site_idPS00126
Number of Residues12
DetailsPDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDVdHpGvsNqF
ChainResidueDetails
AHIS366-PHE377

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q07343
ChainResidueDetails
AGLY462
BGLY462

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7
ChainResidueDetails
AGLY462
BGLY462

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:2PW3
ChainResidueDetails
ALEU466
BLEU466

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3
ChainResidueDetails
BILE502
AILE502

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW
ChainResidueDetails
BMET503
AMET503

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692
ChainResidueDetails
BLYS299
BPHE301
ALYS299
APHE301

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
AASN375
BASN375
BGLU348
AGLU348

site_idSWS_FT_FI8
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
ChainResidueDetails
ALEU387
BLEU387

218500

PDB entries from 2024-04-17

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