1Y10
Mycobacterial adenylyl cyclase Rv1264, holoenzyme, inhibited state
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004016 | molecular_function | adenylate cyclase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0006171 | biological_process | cAMP biosynthetic process |
A | 0008289 | molecular_function | lipid binding |
A | 0009190 | biological_process | cyclic nucleotide biosynthetic process |
A | 0009268 | biological_process | response to pH |
A | 0010855 | molecular_function | adenylate cyclase inhibitor activity |
A | 0016829 | molecular_function | lyase activity |
A | 0030145 | molecular_function | manganese ion binding |
A | 0035556 | biological_process | intracellular signal transduction |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0004016 | molecular_function | adenylate cyclase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0006171 | biological_process | cAMP biosynthetic process |
B | 0008289 | molecular_function | lipid binding |
B | 0009190 | biological_process | cyclic nucleotide biosynthetic process |
B | 0009268 | biological_process | response to pH |
B | 0010855 | molecular_function | adenylate cyclase inhibitor activity |
B | 0016829 | molecular_function | lyase activity |
B | 0030145 | molecular_function | manganese ion binding |
B | 0035556 | biological_process | intracellular signal transduction |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0004016 | molecular_function | adenylate cyclase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005524 | molecular_function | ATP binding |
C | 0006171 | biological_process | cAMP biosynthetic process |
C | 0008289 | molecular_function | lipid binding |
C | 0009190 | biological_process | cyclic nucleotide biosynthetic process |
C | 0009268 | biological_process | response to pH |
C | 0010855 | molecular_function | adenylate cyclase inhibitor activity |
C | 0016829 | molecular_function | lyase activity |
C | 0030145 | molecular_function | manganese ion binding |
C | 0035556 | biological_process | intracellular signal transduction |
C | 0042803 | molecular_function | protein homodimerization activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0004016 | molecular_function | adenylate cyclase activity |
D | 0005515 | molecular_function | protein binding |
D | 0005524 | molecular_function | ATP binding |
D | 0006171 | biological_process | cAMP biosynthetic process |
D | 0008289 | molecular_function | lipid binding |
D | 0009190 | biological_process | cyclic nucleotide biosynthetic process |
D | 0009268 | biological_process | response to pH |
D | 0010855 | molecular_function | adenylate cyclase inhibitor activity |
D | 0016829 | molecular_function | lyase activity |
D | 0030145 | molecular_function | manganese ion binding |
D | 0035556 | biological_process | intracellular signal transduction |
D | 0042803 | molecular_function | protein homodimerization activity |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA C 604 |
Chain | Residue |
C | ASP265 |
C | HOH690 |
D | GLU136 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA D 605 |
Chain | Residue |
D | ASP222 |
D | LEU223 |
D | ASP265 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA B 606 |
Chain | Residue |
B | ASP265 |
A | HOH673 |
B | ASP222 |
B | LEU223 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 607 |
Chain | Residue |
A | ASP222 |
A | LEU223 |
A | ASP265 |
A | ARG298 |
A | HOH669 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 608 |
Chain | Residue |
A | GLU136 |
A | HOH673 |
B | ASP222 |
B | ASP265 |
B | HOH661 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 609 |
Chain | Residue |
A | GLU44 |
A | HOH624 |
A | HOH653 |
D | GLU44 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CA D 610 |
Chain | Residue |
C | HOH708 |
D | GLU195 |
site_id | AC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CA D 611 |
Chain | Residue |
D | ASN319 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE 1PE A 601 |
Chain | Residue |
A | LEU53 |
A | MET154 |
B | PHE117 |
B | VAL130 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE 1PE B 602 |
Chain | Residue |
A | MET193 |
B | MET145 |
B | SER167 |
B | HOH706 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE 1PE D 603 |
Chain | Residue |
C | PHE117 |
C | VAL130 |
C | MET193 |
D | ALA149 |
D | LEU150 |
D | HOH730 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000305|PubMed:11839758 |
Chain | Residue | Details |
A | ASP222 | |
A | ASP265 | |
B | ASP222 | |
B | ASP265 | |
C | ASP222 | |
C | ASP265 | |
D | ASP222 | |
D | ASP265 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | LYS261 | |
D | LYS261 | |
D | ARG298 | |
D | ASP312 | |
A | ARG298 | |
A | ASP312 | |
B | LYS261 | |
B | ARG298 | |
B | ASP312 | |
C | LYS261 | |
C | ARG298 | |
C | ASP312 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609 |
Chain | Residue | Details |
A | THR2 | |
B | THR2 | |
C | THR2 | |
D | THR2 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ab8 |
Chain | Residue | Details |
A | ARG323 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ab8 |
Chain | Residue | Details |
B | ARG323 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ab8 |
Chain | Residue | Details |
C | ARG323 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ab8 |
Chain | Residue | Details |
D | ARG323 |