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6F8T

Crystal structure of the PDE4D catalytic domain in complex with GEBR-4a

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 Residues7
Detailsbinding site for residue ZN A 601
ChainResidue
AHIS330
AHIS366
AASP367
AASP484
AMG602
AHOH756
AHOH840

site_idAC2
Number of Residues7
Detailsbinding site for residue MG A 602
ChainResidue
AHOH756
AHOH803
AHOH857
AHOH867
AHOH933
AASP367
AZN601

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 603
ChainResidue
ATYR325
AHIS330
AASP333
AASN487
ATRP498

site_idAC4
Number of Residues1
Detailsbinding site for residue MG A 604
ChainResidue
AHOH714

site_idAC5
Number of Residues6
Detailsbinding site for residue MG A 605
ChainResidue
AASP467
AASP471
AHIS527
AHOH779
AHOH780
AHOH814

site_idAC6
Number of Residues16
Detailsbinding site for residue CZT A 606
ChainResidue
ATYR325
AHIS326
AMET439
AASN487
ATHR499
AILE502
APHE506
AMET523
ACYS524
AGLN535
APHE538
AHOH707
AHOH757
AHOH766
AHOH819
AHOH829

site_idAC7
Number of Residues6
Detailsbinding site for residue ZN B 601
ChainResidue
BHIS330
BHIS366
BASP367
BASP484
BHOH726
BHOH838

site_idAC8
Number of Residues6
Detailsbinding site for residue MG B 602
ChainResidue
BASP367
BHOH726
BHOH758
BHOH832
BHOH848
BHOH868

site_idAC9
Number of Residues14
Detailsbinding site for residue CZT B 603
ChainResidue
BTYR325
BSER374
BASN487
BTHR499
BILE502
BPHE506
BMET523
BCYS524
BGLN535
BPHE538
BHOH714
BHOH772
BHOH828
BHOH863

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
AILE502
BILE502

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

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

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

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

222415

PDB entries from 2024-07-10

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