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4P2M

Swapped Dimer of Mycobacterial Adenylyl cyclase Rv1625c: Form 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0009190biological_processcyclic nucleotide biosynthetic process
A0016849molecular_functionphosphorus-oxygen lyase activity
A0035556biological_processintracellular signal transduction
B0009190biological_processcyclic nucleotide biosynthetic process
B0016849molecular_functionphosphorus-oxygen lyase activity
B0035556biological_processintracellular signal transduction
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue SO4 A 501
ChainResidue
AARG274
AARG278
BARG274
BARG278

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 502
ChainResidue
BVAL426
AARG405
AHOH602
AHOH607
AHOH610
BLYS411

site_idAC3
Number of Residues3
Detailsbinding site for residue PEG A 503
ChainResidue
BVAL356
BPHE362
BPEG504

site_idAC4
Number of Residues4
Detailsbinding site for residue PEG A 504
ChainResidue
AGLU391
AARG395
BTHR349
BGLY350

site_idAC5
Number of Residues1
Detailsbinding site for residue PEG A 505
ChainResidue
AARG417

site_idAC6
Number of Residues6
Detailsbinding site for residue PEG A 506
ChainResidue
ALYS246
AASP248
APRO351
AVAL353
BGLY368
BASP369

site_idAC7
Number of Residues5
Detailsbinding site for residue PEG A 507
ChainResidue
AHIS290
AARG312
AASP314
AALA318
AASP321

site_idAC8
Number of Residues3
Detailsbinding site for residue PEG B 501
ChainResidue
BASP314
BALA318
BASP321

site_idAC9
Number of Residues6
Detailsbinding site for residue PEG B 502
ChainResidue
BASP284
BVAL287
BASP288
BLEU292
BGLU293
BLYS294

site_idAD1
Number of Residues5
Detailsbinding site for residue PEG B 503
ChainResidue
BLYS246
BTYR247
BASP248
BPRO351
BVAL352

site_idAD2
Number of Residues3
Detailsbinding site for residue PEG B 504
ChainResidue
APEG503
BARG360
BPHE362

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:11447108
ChainResidueDetails
AASP256
AASP300
BASP256
BASP300

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PDB entries from 2024-06-12

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