3OJI
X-ray crystal structure of the Py13 -pyrabactin complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004864 | molecular_function | protein phosphatase inhibitor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0009738 | biological_process | abscisic acid-activated signaling pathway |
| A | 0010427 | molecular_function | abscisic acid binding |
| A | 0038023 | molecular_function | signaling receptor activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0062049 | cellular_component | protein phosphatase inhibitor complex |
| B | 0004864 | molecular_function | protein phosphatase inhibitor activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0009738 | biological_process | abscisic acid-activated signaling pathway |
| B | 0010427 | molecular_function | abscisic acid binding |
| B | 0038023 | molecular_function | signaling receptor activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0062049 | cellular_component | protein phosphatase inhibitor complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PYV A 210 |
| Chain | Residue |
| A | PHE81 |
| A | HOH312 |
| A | ILE82 |
| A | LEU111 |
| A | ALA113 |
| A | SER116 |
| A | GLU118 |
| A | LEU141 |
| A | PHE188 |
| A | HOH307 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PYV B 210 |
| Chain | Residue |
| B | SO42 |
| B | PHE81 |
| B | ILE82 |
| B | GLU118 |
| B | LEU141 |
| B | TYR144 |
| B | VAL192 |
| B | HOH217 |
| B | HOH270 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1 |
| Chain | Residue |
| A | HIS63 |
| B | ALA113 |
| B | SER114 |
| B | THR115 |
| B | GLU138 |
| B | HIS139 |
| B | ARG140 |
| B | HOH244 |
| B | HOH286 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2 |
| Chain | Residue |
| B | LYS79 |
| B | PHE132 |
| B | TYR144 |
| B | SER146 |
| B | GLU170 |
| B | ASN196 |
| B | PYV210 |
| B | HOH270 |
| B | HOH339 |
| B | HOH377 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22579247, ECO:0000269|PubMed:23844015, ECO:0007744|PDB:4DS8, ECO:0007744|PDB:4DSB, ECO:0007744|PDB:4DSC, ECO:0007744|PDB:4JDA |
| Chain | Residue | Details |
| A | LYS79 | |
| B | LYS79 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:O49686 |
| Chain | Residue | Details |
| A | ALA113 | |
| A | GLU170 | |
| B | ALA113 | |
| B | GLU170 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22579247, ECO:0007744|PDB:4DSC |
| Chain | Residue | Details |
| A | ARG140 | |
| B | ARG140 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | SITE: Involved in interactions with PP2Cs => ECO:0000250|UniProtKB:O49686 |
| Chain | Residue | Details |
| A | PRO112 | |
| A | THR181 | |
| B | PRO112 | |
| B | THR181 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Involved in ABA binding => ECO:0000250|UniProtKB:Q84MC7 |
| Chain | Residue | Details |
| A | VAL189 | |
| B | VAL189 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Involved in the cis- to trans-homodimer conformation in the presence of ABA => ECO:0000269|PubMed:22579247 |
| Chain | Residue | Details |
| A | SER195 | |
| B | SER195 |
