3E8C
Crystal structures of the kinase domain of PKA in complex with ATP-competitive inhibitors
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001669 | cellular_component | acrosomal vesicle |
| A | 0001707 | biological_process | mesoderm formation |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0004679 | molecular_function | AMP-activated protein kinase activity |
| A | 0004691 | molecular_function | cAMP-dependent protein kinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005952 | cellular_component | cAMP-dependent protein kinase complex |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0010737 | biological_process | protein kinase A signaling |
| A | 0018105 | biological_process | peptidyl-serine phosphorylation |
| A | 0019904 | molecular_function | protein domain specific binding |
| A | 0031594 | cellular_component | neuromuscular junction |
| A | 0034237 | molecular_function | protein kinase A regulatory subunit binding |
| A | 0034605 | biological_process | cellular response to heat |
| A | 0036126 | cellular_component | sperm flagellum |
| A | 0048471 | cellular_component | perinuclear region of cytoplasm |
| A | 0106310 | molecular_function | protein serine kinase activity |
| A | 1904262 | biological_process | negative regulation of TORC1 signaling |
| B | 0001669 | cellular_component | acrosomal vesicle |
| B | 0001707 | biological_process | mesoderm formation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0004679 | molecular_function | AMP-activated protein kinase activity |
| B | 0004691 | molecular_function | cAMP-dependent protein kinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005952 | cellular_component | cAMP-dependent protein kinase complex |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0010737 | biological_process | protein kinase A signaling |
| B | 0018105 | biological_process | peptidyl-serine phosphorylation |
| B | 0019904 | molecular_function | protein domain specific binding |
| B | 0031594 | cellular_component | neuromuscular junction |
| B | 0034237 | molecular_function | protein kinase A regulatory subunit binding |
| B | 0034605 | biological_process | cellular response to heat |
| B | 0036126 | cellular_component | sperm flagellum |
| B | 0048471 | cellular_component | perinuclear region of cytoplasm |
| B | 0106310 | molecular_function | protein serine kinase activity |
| B | 1904262 | biological_process | negative regulation of TORC1 signaling |
| C | 0001669 | cellular_component | acrosomal vesicle |
| C | 0001707 | biological_process | mesoderm formation |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004674 | molecular_function | protein serine/threonine kinase activity |
| C | 0004679 | molecular_function | AMP-activated protein kinase activity |
| C | 0004691 | molecular_function | cAMP-dependent protein kinase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005829 | cellular_component | cytosol |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0005952 | cellular_component | cAMP-dependent protein kinase complex |
| C | 0006468 | biological_process | protein phosphorylation |
| C | 0010737 | biological_process | protein kinase A signaling |
| C | 0018105 | biological_process | peptidyl-serine phosphorylation |
| C | 0019904 | molecular_function | protein domain specific binding |
| C | 0031594 | cellular_component | neuromuscular junction |
| C | 0034237 | molecular_function | protein kinase A regulatory subunit binding |
| C | 0034605 | biological_process | cellular response to heat |
| C | 0036126 | cellular_component | sperm flagellum |
| C | 0048471 | cellular_component | perinuclear region of cytoplasm |
| C | 0106310 | molecular_function | protein serine kinase activity |
| C | 1904262 | biological_process | negative regulation of TORC1 signaling |
| D | 0001669 | cellular_component | acrosomal vesicle |
| D | 0001707 | biological_process | mesoderm formation |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0004674 | molecular_function | protein serine/threonine kinase activity |
| D | 0004679 | molecular_function | AMP-activated protein kinase activity |
| D | 0004691 | molecular_function | cAMP-dependent protein kinase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005829 | cellular_component | cytosol |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0005952 | cellular_component | cAMP-dependent protein kinase complex |
| D | 0006468 | biological_process | protein phosphorylation |
| D | 0010737 | biological_process | protein kinase A signaling |
| D | 0018105 | biological_process | peptidyl-serine phosphorylation |
| D | 0019904 | molecular_function | protein domain specific binding |
| D | 0031594 | cellular_component | neuromuscular junction |
| D | 0034237 | molecular_function | protein kinase A regulatory subunit binding |
| D | 0034605 | biological_process | cellular response to heat |
| D | 0036126 | cellular_component | sperm flagellum |
| D | 0048471 | cellular_component | perinuclear region of cytoplasm |
| D | 0106310 | molecular_function | protein serine kinase activity |
| D | 1904262 | biological_process | negative regulation of TORC1 signaling |
| E | 0001669 | cellular_component | acrosomal vesicle |
| E | 0001707 | biological_process | mesoderm formation |
| E | 0004672 | molecular_function | protein kinase activity |
| E | 0004674 | molecular_function | protein serine/threonine kinase activity |
| E | 0004679 | molecular_function | AMP-activated protein kinase activity |
| E | 0004691 | molecular_function | cAMP-dependent protein kinase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005634 | cellular_component | nucleus |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005739 | cellular_component | mitochondrion |
| E | 0005829 | cellular_component | cytosol |
| E | 0005886 | cellular_component | plasma membrane |
| E | 0005952 | cellular_component | cAMP-dependent protein kinase complex |
| E | 0006468 | biological_process | protein phosphorylation |
| E | 0010737 | biological_process | protein kinase A signaling |
| E | 0018105 | biological_process | peptidyl-serine phosphorylation |
| E | 0019904 | molecular_function | protein domain specific binding |
| E | 0031594 | cellular_component | neuromuscular junction |
| E | 0034237 | molecular_function | protein kinase A regulatory subunit binding |
| E | 0034605 | biological_process | cellular response to heat |
| E | 0036126 | cellular_component | sperm flagellum |
| E | 0048471 | cellular_component | perinuclear region of cytoplasm |
| E | 0106310 | molecular_function | protein serine kinase activity |
| E | 1904262 | biological_process | negative regulation of TORC1 signaling |
| F | 0001669 | cellular_component | acrosomal vesicle |
| F | 0001707 | biological_process | mesoderm formation |
| F | 0004672 | molecular_function | protein kinase activity |
| F | 0004674 | molecular_function | protein serine/threonine kinase activity |
| F | 0004679 | molecular_function | AMP-activated protein kinase activity |
| F | 0004691 | molecular_function | cAMP-dependent protein kinase activity |
| F | 0005515 | molecular_function | protein binding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005634 | cellular_component | nucleus |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005739 | cellular_component | mitochondrion |
| F | 0005829 | cellular_component | cytosol |
| F | 0005886 | cellular_component | plasma membrane |
| F | 0005952 | cellular_component | cAMP-dependent protein kinase complex |
| F | 0006468 | biological_process | protein phosphorylation |
| F | 0010737 | biological_process | protein kinase A signaling |
| F | 0018105 | biological_process | peptidyl-serine phosphorylation |
| F | 0019904 | molecular_function | protein domain specific binding |
| F | 0031594 | cellular_component | neuromuscular junction |
| F | 0034237 | molecular_function | protein kinase A regulatory subunit binding |
| F | 0034605 | biological_process | cellular response to heat |
| F | 0036126 | cellular_component | sperm flagellum |
| F | 0048471 | cellular_component | perinuclear region of cytoplasm |
| F | 0106310 | molecular_function | protein serine kinase activity |
| F | 1904262 | biological_process | negative regulation of TORC1 signaling |
| G | 0004862 | molecular_function | cAMP-dependent protein kinase inhibitor activity |
| G | 0006469 | biological_process | negative regulation of protein kinase activity |
| H | 0004862 | molecular_function | cAMP-dependent protein kinase inhibitor activity |
| H | 0006469 | biological_process | negative regulation of protein kinase activity |
| I | 0004862 | molecular_function | cAMP-dependent protein kinase inhibitor activity |
| I | 0006469 | biological_process | negative regulation of protein kinase activity |
| J | 0004862 | molecular_function | cAMP-dependent protein kinase inhibitor activity |
| J | 0006469 | biological_process | negative regulation of protein kinase activity |
| K | 0004862 | molecular_function | cAMP-dependent protein kinase inhibitor activity |
| K | 0006469 | biological_process | negative regulation of protein kinase activity |
| L | 0004862 | molecular_function | cAMP-dependent protein kinase inhibitor activity |
| L | 0006469 | biological_process | negative regulation of protein kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE G96 A 351 |
| Chain | Residue |
| A | LEU49 |
| A | MET120 |
| A | GLU121 |
| A | TYR122 |
| A | VAL123 |
| A | LEU173 |
| A | THR183 |
| A | ASP184 |
| A | PHE185 |
| A | PHE327 |
| A | GLY52 |
| A | PHE54 |
| A | GLY55 |
| A | ARG56 |
| A | LYS72 |
| A | GLU91 |
| A | LEU95 |
| A | VAL104 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE G96 B 351 |
| Chain | Residue |
| B | GLY50 |
| B | GLY52 |
| B | PHE54 |
| B | GLY55 |
| B | ARG56 |
| B | VAL57 |
| B | LYS72 |
| B | LEU74 |
| B | GLU91 |
| B | LEU95 |
| B | VAL104 |
| B | MET120 |
| B | GLU121 |
| B | TYR122 |
| B | VAL123 |
| B | LEU173 |
| B | THR183 |
| B | ASP184 |
| B | PHE185 |
| B | PHE327 |
| B | HOH706 |
| B | HOH728 |
| B | HOH752 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE G96 C 351 |
| Chain | Residue |
| C | LEU49 |
| C | PHE54 |
| C | GLY55 |
| C | ARG56 |
| C | VAL57 |
| C | LYS72 |
| C | LEU74 |
| C | GLU91 |
| C | LEU95 |
| C | VAL104 |
| C | MET120 |
| C | GLU121 |
| C | TYR122 |
| C | VAL123 |
| C | LEU173 |
| C | THR183 |
| C | ASP184 |
| C | PHE185 |
| C | PHE327 |
| C | HOH392 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE G96 D 351 |
| Chain | Residue |
| D | LEU49 |
| D | GLY50 |
| D | GLY52 |
| D | PHE54 |
| D | GLY55 |
| D | ARG56 |
| D | VAL57 |
| D | LYS72 |
| D | LEU74 |
| D | GLU91 |
| D | LEU95 |
| D | VAL104 |
| D | MET120 |
| D | GLU121 |
| D | TYR122 |
| D | VAL123 |
| D | LEU173 |
| D | THR183 |
| D | ASP184 |
| D | PHE185 |
| D | PHE327 |
| D | HOH389 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE G96 E 351 |
| Chain | Residue |
| E | THR183 |
| E | ASP184 |
| E | PHE185 |
| E | PHE327 |
| E | LEU49 |
| E | GLY52 |
| E | PHE54 |
| E | GLY55 |
| E | ARG56 |
| E | VAL57 |
| E | LYS72 |
| E | LEU74 |
| E | GLU91 |
| E | LEU95 |
| E | VAL104 |
| E | MET120 |
| E | GLU121 |
| E | TYR122 |
| E | VAL123 |
| E | LEU173 |
| site_id | AC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE G96 F 351 |
| Chain | Residue |
| F | LEU49 |
| F | PHE54 |
| F | GLY55 |
| F | ARG56 |
| F | VAL57 |
| F | LYS72 |
| F | LEU74 |
| F | GLU91 |
| F | LEU95 |
| F | VAL104 |
| F | MET120 |
| F | GLU121 |
| F | TYR122 |
| F | VAL123 |
| F | LEU173 |
| F | THR183 |
| F | ASP184 |
| F | PHE185 |
| F | PHE327 |
| F | HOH397 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhmetgnh..........YAMK |
| Chain | Residue | Details |
| A | LEU49-LYS72 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI |
| Chain | Residue | Details |
| A | LEU162-ILE174 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | SITE: Important for inhibition => ECO:0000250 |
| Chain | Residue | Details |
| G | ARG15 | |
| J | ARG15 | |
| J | ARG18 | |
| J | ARG19 | |
| K | ARG15 | |
| K | ARG18 | |
| K | ARG19 | |
| L | ARG15 | |
| L | ARG18 | |
| L | ARG19 | |
| G | ARG18 | |
| G | ARG19 | |
| H | ARG15 | |
| H | ARG18 | |
| H | ARG19 | |
| I | ARG15 | |
| I | ARG18 | |
| I | ARG19 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LEU49 | |
| E | LYS72 | |
| F | LEU49 | |
| F | LYS72 | |
| A | LYS72 | |
| B | LEU49 | |
| B | LYS72 | |
| C | LEU49 | |
| C | LYS72 | |
| D | LEU49 | |
| D | LYS72 | |
| E | LEU49 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | GLU121 | |
| E | LYS168 | |
| F | GLU121 | |
| F | LYS168 | |
| A | LYS168 | |
| B | GLU121 | |
| B | LYS168 | |
| C | GLU121 | |
| C | LYS168 | |
| D | GLU121 | |
| D | LYS168 | |
| E | GLU121 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | MOD_RES: Deamidated asparagine; partial => ECO:0000269|PubMed:10684253, ECO:0000269|PubMed:11152138, ECO:0000269|PubMed:9521123 |
| Chain | Residue | Details |
| A | ASN2 | |
| B | ASN2 | |
| C | ASN2 | |
| D | ASN2 | |
| E | ASN2 | |
| F | ASN2 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P05132 |
| Chain | Residue | Details |
| A | SEP10 | |
| B | SEP10 | |
| C | SEP10 | |
| D | SEP10 | |
| E | SEP10 | |
| F | SEP10 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P17612 |
| Chain | Residue | Details |
| A | THR48 | |
| E | THR195 | |
| F | THR48 | |
| F | THR195 | |
| A | THR195 | |
| B | THR48 | |
| B | THR195 | |
| C | THR48 | |
| C | THR195 | |
| D | THR48 | |
| D | THR195 | |
| E | THR48 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P05132 |
| Chain | Residue | Details |
| A | SER139 | |
| B | SER139 | |
| C | SER139 | |
| D | SER139 | |
| E | SER139 | |
| F | SER139 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:6262777 |
| Chain | Residue | Details |
| A | TPO197 | |
| B | TPO197 | |
| C | TPO197 | |
| D | TPO197 | |
| E | TPO197 | |
| F | TPO197 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P05132 |
| Chain | Residue | Details |
| A | TYR330 | |
| B | TYR330 | |
| C | TYR330 | |
| D | TYR330 | |
| E | TYR330 | |
| F | TYR330 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:6262777 |
| Chain | Residue | Details |
| A | SEP338 | |
| B | SEP338 | |
| C | SEP338 | |
| D | SEP338 | |
| E | SEP338 | |
| F | SEP338 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 6 |
| Details | LIPID: N-myristoyl glycine => ECO:0000269|PubMed:6262777 |
| Chain | Residue | Details |
| A | GLY1 | |
| B | GLY1 | |
| C | GLY1 | |
| D | GLY1 | |
| E | GLY1 | |
| F | GLY1 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | GLU170 | |
| A | ASP166 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | GLU170 | |
| B | ASP166 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | GLU170 | |
| C | ASP166 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | GLU170 | |
| D | ASP166 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| E | GLU170 | |
| E | ASP166 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| F | GLU170 | |
| F | ASP166 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP166 | |
| A | LYS168 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP166 | |
| B | LYS168 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | ASP166 | |
| C | LYS168 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | ASP166 | |
| D | LYS168 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| E | ASP166 | |
| E | LYS168 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| F | ASP166 | |
| F | LYS168 |
| site_id | CSA13 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | THR201 | |
| A | ASP166 | |
| A | LYS168 |
| site_id | CSA14 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | THR201 | |
| B | ASP166 | |
| B | LYS168 |
| site_id | CSA15 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | THR201 | |
| C | ASP166 | |
| C | LYS168 |
| site_id | CSA16 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | THR201 | |
| D | ASP166 | |
| D | LYS168 |
| site_id | CSA17 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| E | THR201 | |
| E | ASP166 | |
| E | LYS168 |
| site_id | CSA18 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| F | THR201 | |
| F | ASP166 | |
| F | LYS168 |
| site_id | CSA19 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP166 | |
| A | ASN171 | |
| A | LYS168 |
| site_id | CSA20 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP166 | |
| B | ASN171 | |
| B | LYS168 |
| site_id | CSA21 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | ASP166 | |
| C | ASN171 | |
| C | LYS168 |
| site_id | CSA22 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | ASP166 | |
| D | ASN171 | |
| D | LYS168 |
| site_id | CSA23 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| E | ASP166 | |
| E | ASN171 | |
| E | LYS168 |
| site_id | CSA24 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| F | ASP166 | |
| F | ASN171 | |
| F | LYS168 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 757 |
| Chain | Residue | Details |
| A | ASP166 | activator, proton acceptor, proton donor |
| A | LYS168 | electrostatic stabiliser, polar interaction |
| A | ASN171 | metal ligand |
| A | ASP184 | metal ligand |
| A | THR201 | electrostatic stabiliser, polar interaction |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 757 |
| Chain | Residue | Details |
| B | ASP166 | activator, proton acceptor, proton donor |
| B | LYS168 | electrostatic stabiliser, polar interaction |
| B | ASN171 | metal ligand |
| B | ASP184 | metal ligand |
| B | THR201 | electrostatic stabiliser, polar interaction |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 757 |
| Chain | Residue | Details |
| C | ASP166 | activator, proton acceptor, proton donor |
| C | LYS168 | electrostatic stabiliser, polar interaction |
| C | ASN171 | metal ligand |
| C | ASP184 | metal ligand |
| C | THR201 | electrostatic stabiliser, polar interaction |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 757 |
| Chain | Residue | Details |
| D | ASP166 | activator, proton acceptor, proton donor |
| D | LYS168 | electrostatic stabiliser, polar interaction |
| D | ASN171 | metal ligand |
| D | ASP184 | metal ligand |
| D | THR201 | electrostatic stabiliser, polar interaction |
| site_id | MCSA5 |
| Number of Residues | 5 |
| Details | M-CSA 757 |
| Chain | Residue | Details |
| E | ASP166 | activator, proton acceptor, proton donor |
| E | LYS168 | electrostatic stabiliser, polar interaction |
| E | ASN171 | metal ligand |
| E | ASP184 | metal ligand |
| E | THR201 | electrostatic stabiliser, polar interaction |
| site_id | MCSA6 |
| Number of Residues | 5 |
| Details | M-CSA 757 |
| Chain | Residue | Details |
| F | ASP166 | activator, proton acceptor, proton donor |
| F | LYS168 | electrostatic stabiliser, polar interaction |
| F | ASN171 | metal ligand |
| F | ASP184 | metal ligand |
| F | THR201 | electrostatic stabiliser, polar interaction |
