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7YZI

Structure of Mycobacterium tuberculosis adenylyl cyclase Rv1625c / Cya

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0001653molecular_functionpeptide receptor activity
A0004016molecular_functionadenylate cyclase activity
A0004383molecular_functionguanylate cyclase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0006171biological_processcAMP biosynthetic process
A0006182biological_processcGMP biosynthetic process
A0007168biological_processreceptor guanylyl cyclase signaling pathway
A0009190biological_processcyclic nucleotide biosynthetic process
A0016829molecular_functionlyase activity
A0016849molecular_functionphosphorus-oxygen lyase activity
A0030145molecular_functionmanganese ion binding
A0035556biological_processintracellular signal transduction
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0001653molecular_functionpeptide receptor activity
B0004016molecular_functionadenylate cyclase activity
B0004383molecular_functionguanylate cyclase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005886cellular_componentplasma membrane
B0006171biological_processcAMP biosynthetic process
B0006182biological_processcGMP biosynthetic process
B0007168biological_processreceptor guanylyl cyclase signaling pathway
B0009190biological_processcyclic nucleotide biosynthetic process
B0016829molecular_functionlyase activity
B0016849molecular_functionphosphorus-oxygen lyase activity
B0030145molecular_functionmanganese ion binding
B0035556biological_processintracellular signal transduction
B0046872molecular_functionmetal ion binding
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 Residues246
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AVAL47-THR69
BALA124-ILE143
BLEU148-VAL167
BSER180-LEU202
ATRP74-LEU93
AGLY98-VAL120
AALA124-ILE143
ALEU148-VAL167
ASER180-LEU202
BVAL47-THR69
BTRP74-LEU93
BGLY98-VAL120

site_idSWS_FT_FI2
Number of Residues480
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255, ECO:0000305|PubMed:11447108
ChainResidueDetails
AARG203-VAL443
BARG203-VAL443

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:11447108
ChainResidueDetails
AASP256
AASP300
BASP256
BASP300

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PDB entries from 2024-07-17

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