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6F6U

Crystal structure of the PDE4D catalytic domain in complex with GEBR-7b

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 MG A 601
ChainResidue
AASP367
AZN602
AHOH783
AHOH799
AHOH821
AHOH875
AHOH893

site_idAC2
Number of Residues7
Detailsbinding site for residue ZN A 602
ChainResidue
AASP367
AASP484
AMG601
AHOH783
AHOH877
AHIS330
AHIS366

site_idAC3
Number of Residues4
Detailsbinding site for residue MG A 603
ChainResidue
AASP264
AASN417
AHOH710
AHOH904

site_idAC4
Number of Residues13
Detailsbinding site for residue CV8 A 604
ChainResidue
ATYR325
ASER374
AMET439
AASN487
ATHR499
AILE502
APHE506
AGLN509
AMET523
ACYS524
AGLN535
APHE538
AHOH786

site_idAC5
Number of Residues8
Detailsbinding site for residue GOL A 605
ChainResidue
AHIS398
AVAL402
AHOH716
AHOH755
AHOH824
BMET388
BTRP571
BSER574

site_idAC6
Number of Residues7
Detailsbinding site for residue MG B 601
ChainResidue
BASP367
BZN602
BHOH767
BHOH780
BHOH835
BHOH838
BHOH857

site_idAC7
Number of Residues7
Detailsbinding site for residue ZN B 602
ChainResidue
BHIS330
BHIS366
BASP367
BASP484
BMG601
BHOH780
BHOH851

site_idAC8
Number of Residues14
Detailsbinding site for residue CV8 B 603
ChainResidue
BTYR325
BMET439
BASN487
BTRP498
BTHR499
BILE502
BMET503
BPHE506
BGLN535
BPHE538
BHOH706
BHOH709
BHOH735
BHOH823

site_idAC9
Number of Residues1
Detailsbinding site for residue GOL B 604
ChainResidue
BHOH717

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
BGLY462
AGLY462

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
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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