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5IV4

Crystal structure of the human soluble adenylyl cyclase in complex with the allosteric inhibitor LRE1

Functional Information from GO Data
ChainGOidnamespacecontents
A0009190biological_processcyclic nucleotide biosynthetic process
A0035556biological_processintracellular signal transduction
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue LRI A 501
ChainResidue
APHE45
ALEU102
APHE165
AVAL167
AVAL172
AVAL175
AARG176
APHE336
AMET337

site_idAC2
Number of Residues3
Detailsbinding site for residue ACT A 502
ChainResidue
AASP278
AASN279
AGLN283

site_idAC3
Number of Residues7
Detailsbinding site for residue ACT A 503
ChainResidue
ALYS95
AHIS164
AASN333
ALYS334
AVAL335
AGOL515
AHOH654

site_idAC4
Number of Residues3
Detailsbinding site for residue EDO A 504
ChainResidue
AGLN409
AHOH606
AHOH609

site_idAC5
Number of Residues3
Detailsbinding site for residue EDO A 505
ChainResidue
AHOH755
AHOH781
AHOH840

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO A 506
ChainResidue
APHE230
ATHR231
ATHR234
AHOH807
AHOH814

site_idAC7
Number of Residues3
Detailsbinding site for residue EDO A 507
ChainResidue
APRO31
AGLY158
AGLU160

site_idAC8
Number of Residues6
Detailsbinding site for residue EDO A 508
ChainResidue
AASN298
APHE336
APHE338
AGLY341
ASER343
AHOH642

site_idAC9
Number of Residues6
Detailsbinding site for residue DMS A 509
ChainResidue
ATYR77
AHIS78
AALA81
ALEU129
APHE130
AHOH951

site_idAD1
Number of Residues4
Detailsbinding site for residue DMS A 510
ChainResidue
AILE88
APHE89
APHE226
APHE230

site_idAD2
Number of Residues5
Detailsbinding site for residue DMS A 511
ChainResidue
AILE24
AGLY27
APHE29
ALEU261
ATYR268

site_idAD3
Number of Residues7
Detailsbinding site for residue DMS A 512
ChainResidue
APHE8
ATRP11
ASER80
AHIS398
ATHR399
AHOH630
AHOH885

site_idAD4
Number of Residues1
Detailsbinding site for residue CL A 513
ChainResidue
AGLN409

site_idAD5
Number of Residues6
Detailsbinding site for residue PEG A 514
ChainResidue
AHIS162
AHIS164
ATYR318
ATHR322
ALYS326
AGLY330

site_idAD6
Number of Residues7
Detailsbinding site for residue GOL A 515
ChainResidue
AHIS19
APHE165
ATYR268
ALYS334
AACT503
AHOH628
AHOH654

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00099
ChainResidueDetails
AILE48
AASP99
AASP47

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:24567411, ECO:0000269|PubMed:24616449, ECO:0007744|PDB:4CLL, ECO:0007744|PDB:4OYZ
ChainResidueDetails
AVAL167
AARG176
AMET337
ALYS95

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:25040695, ECO:0000305|PubMed:24567411, ECO:0000305|PubMed:24616449, ECO:0007744|PDB:4USW
ChainResidueDetails
ALYS144
AVAL406

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:24567411, ECO:0000305|PubMed:24616449, ECO:0000305|PubMed:25040695
ChainResidueDetails
AASN412

220472

PDB entries from 2024-05-29

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