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4P2F

Monomeric form of a single mutant (F363R) of Mycobacterial Adenylyl cyclase Rv1625c

Functional Information from GO Data
ChainGOidnamespacecontents
A0009190biological_processcyclic nucleotide biosynthetic process
A0016849molecular_functionphosphorus-oxygen lyase activity
A0035556biological_processintracellular signal transduction
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue EDO A 501
ChainResidue
AILE243
AALA244
AASP245
AARG278

site_idAC2
Number of Residues6
Detailsbinding site for residue EDO A 502
ChainResidue
AHOH684
ASER306
AGLY307
AVAL308
APRO309
AARG310

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 503
ChainResidue
ALEU324
ATHR327
AASN328
AGLY384
AGLN385
AILE422

site_idAC4
Number of Residues7
Detailsbinding site for residue EDO A 504
ChainResidue
AARG278
APRO309
ALEU333
ALYS334
AEDO507
AHOH606
AHOH645

site_idAC5
Number of Residues3
Detailsbinding site for residue EDO A 505
ChainResidue
AASP256
AGLY259
AGLU285

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO A 506
ChainResidue
AASP288
AGLN289
AGLY291
AARG344
ASER379

site_idAC7
Number of Residues8
Detailsbinding site for residue EDO A 507
ChainResidue
AALA244
AASP245
ATYR247
AARG278
AALA354
AGLY355
ATYR364
AEDO504

site_idAC8
Number of Residues4
Detailsbinding site for residue EDO A 508
ChainResidue
ALYS246
ATYR247
AASP248
AHOH691

site_idAC9
Number of Residues4
Detailsbinding site for residue EDO A 509
ChainResidue
AASP284
AASP288
AHOH615
AHOH658

site_idAD1
Number of Residues5
Detailsbinding site for residue EDO A 510
ChainResidue
AARG376
APRO389
AASP390
AARG417
AHOH631

site_idAD2
Number of Residues3
Detailsbinding site for residue EDO A 511
ChainResidue
APRO311
AARG376
AHOH610

site_idAD3
Number of Residues4
Detailsbinding site for residue EDO A 512
ChainResidue
AARG310
APRO311
AARG312
AHOH684

site_idAD4
Number of Residues6
Detailsbinding site for residue EDO A 513
ChainResidue
ATYR393
ALYS397
APHE400
AVAL401
ALEU402
AHOH657

site_idAD5
Number of Residues5
Detailsbinding site for residue EDO A 514
ChainResidue
AGLN387
AARG405
AGLY406
AMET416
ATHR418

site_idAD6
Number of Residues7
Detailsbinding site for residue EDO A 515
ChainResidue
AVAL297
AMET303
AARG337
AASP365
AVAL366
AVAL371
AHOH623

site_idAD7
Number of Residues5
Detailsbinding site for residue EDO A 516
ChainResidue
AGLU239
AASN241
AASP335
AASN339
AEDO518

site_idAD8
Number of Residues6
Detailsbinding site for residue EDO A 517
ChainResidue
AASP277
ATYR280
ASER281
AASP284
ALYS294
AHOH677

site_idAD9
Number of Residues4
Detailsbinding site for residue EDO A 518
ChainResidue
AASN241
AARG337
ATRP367
AEDO516

site_idAE1
Number of Residues6
Detailsbinding site for residue PEG A 519
ChainResidue
AGLN289
AHIS290
AARG344
ASER379
AASP381
AHOH607

site_idAE2
Number of Residues3
Detailsbinding site for residue GOL A 520
ChainResidue
AGLY423
AARG424
AASN328

Functional Information from PROSITE/UniProt
site_idPS00452
Number of Residues24
DetailsGUANYLATE_CYCLASE_1 Guanylate cyclase signature. GVV.GsrrfrYdVWGDAVNvasrmE
ChainResidueDetails
AGLY355-GLU378

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:11447108
ChainResidueDetails
AASP256
AASP300

224572

PDB entries from 2024-09-04

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