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6NJI

Crystal Structure of the PDE4D Catalytic Domain and UCR2 Regulatory Helix with T-49

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 700
ChainResidue
AHIS330
AHIS366
AASP367
AASP484
AMG701
AHOH805
AHOH822

site_idAC2
Number of Residues7
Detailsbinding site for residue MG A 701
ChainResidue
AHOH802
AHOH805
AHOH830
AHOH842
AHOH846
AASP367
AZN700

site_idAC3
Number of Residues7
Detailsbinding site for residue KR4 A 702
ChainResidue
AASN487
ATHR499
AGLN535
APHE538
APHE599
AHOH807
AHOH820

site_idAC4
Number of Residues6
Detailsbinding site for residue ZN B 700
ChainResidue
BHIS330
BHIS366
BASP367
BASP484
BHOH805
BHOH810

site_idAC5
Number of Residues6
Detailsbinding site for residue MG B 701
ChainResidue
BASP367
BHOH805
BHOH807
BHOH813
BHOH816
BHOH822

site_idAC6
Number of Residues7
Detailsbinding site for residue KR4 B 702
ChainResidue
BASN487
BTHR499
BGLN535
BPHE538
BPHE599
BHOH804
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
ALEU387
BLEU387

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7
ChainResidueDetails
ALEU387
AGLU548
BLEU387
BGLU548

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
AASP391
BASP391

site_idSWS_FT_FI4
Number of Residues4
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
AARG427
APRO545
BARG427
BPRO545

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW
ChainResidueDetails
ALYS428
BLYS428

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
APHE273
ATHR300
BPHE273
BTHR300

site_idSWS_FT_FI7
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
ChainResidueDetails
ALEU312
BLEU312

217705

數據於2024-03-27公開中

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