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 |
| 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 |
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 | 8 |
| Details | Motif: {"description":"Gate loop","evidences":[{"source":"UniProtKB","id":"Q8VZS8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Motif: {"description":"Latch loop","evidences":[{"source":"UniProtKB","id":"Q8VZS8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22579247","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23844015","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4DS8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4DSB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4DSC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JDA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O49686","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22579247","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4DSC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Site: {"description":"Involved in interactions with PP2Cs","evidences":[{"source":"UniProtKB","id":"O49686","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Site: {"description":"Involved in ABA binding","evidences":[{"source":"UniProtKB","id":"Q84MC7","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Site: {"description":"Involved in the cis- to trans-homodimer conformation in the presence of ABA","evidences":[{"source":"PubMed","id":"22579247","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
