3C0V
Crystal structure of cytokinin-specific binding protein in complex with cytokinin and Ta6Br12
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004864 | molecular_function | protein phosphatase inhibitor activity |
A | 0006952 | biological_process | defense response |
A | 0009738 | biological_process | abscisic acid-activated signaling pathway |
A | 0010331 | molecular_function | gibberellin binding |
A | 0010427 | molecular_function | abscisic acid binding |
A | 0038023 | molecular_function | signaling receptor activity |
A | 0044373 | molecular_function | cytokinin binding |
B | 0004864 | molecular_function | protein phosphatase inhibitor activity |
B | 0006952 | biological_process | defense response |
B | 0009738 | biological_process | abscisic acid-activated signaling pathway |
B | 0010331 | molecular_function | gibberellin binding |
B | 0010427 | molecular_function | abscisic acid binding |
B | 0038023 | molecular_function | signaling receptor activity |
B | 0044373 | molecular_function | cytokinin binding |
C | 0004864 | molecular_function | protein phosphatase inhibitor activity |
C | 0006952 | biological_process | defense response |
C | 0009738 | biological_process | abscisic acid-activated signaling pathway |
C | 0010331 | molecular_function | gibberellin binding |
C | 0010427 | molecular_function | abscisic acid binding |
C | 0038023 | molecular_function | signaling receptor activity |
C | 0044373 | molecular_function | cytokinin binding |
D | 0004864 | molecular_function | protein phosphatase inhibitor activity |
D | 0006952 | biological_process | defense response |
D | 0009738 | biological_process | abscisic acid-activated signaling pathway |
D | 0010331 | molecular_function | gibberellin binding |
D | 0010427 | molecular_function | abscisic acid binding |
D | 0038023 | molecular_function | signaling receptor activity |
D | 0044373 | molecular_function | cytokinin binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 156 |
Chain | Residue |
B | ASP123 |
B | ILE126 |
B | HOH172 |
B | HOH208 |
B | HOH255 |
B | HOH256 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA C 156 |
Chain | Residue |
C | HOH243 |
C | HOH272 |
C | HOH314 |
C | SER124 |
C | ILE126 |
C | HOH203 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ZEA A 156 |
Chain | Residue |
A | LEU22 |
A | PHE26 |
A | GLU69 |
A | THR139 |
A | TYR142 |
A | ZEA157 |
A | HOH179 |
A | HOH241 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ZEA A 157 |
Chain | Residue |
A | LEU34 |
A | ILE37 |
A | PHE58 |
A | VAL62 |
A | GLN67 |
A | GLY89 |
A | TYR90 |
A | GLN93 |
A | ZEA156 |
A | HOH240 |
A | HOH241 |
A | HOH244 |
D | TBR158 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ZEA B 157 |
Chain | Residue |
B | LEU22 |
B | PHE26 |
B | GLN67 |
B | GLU69 |
B | THR100 |
B | THR139 |
B | TYR142 |
B | ZEA158 |
B | HOH163 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ZEA B 158 |
Chain | Residue |
B | PHE56 |
B | GLN67 |
B | GLU69 |
B | TYR90 |
B | ZEA157 |
B | HOH261 |
B | HOH262 |
B | HOH284 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ZEA D 156 |
Chain | Residue |
D | LEU22 |
D | PHE56 |
D | GLN67 |
D | GLU69 |
D | THR139 |
D | TYR142 |
D | ZEA157 |
D | HOH231 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ZEA D 157 |
Chain | Residue |
D | LEU34 |
D | PHE56 |
D | PRO64 |
D | GLN67 |
D | GLY89 |
D | TYR90 |
D | GLN93 |
D | ZEA156 |
D | HOH255 |
site_id | AC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TBR A 158 |
Chain | Residue |
A | ASP40 |
A | GLN42 |
A | ASN57 |
A | TBR159 |
A | HOH277 |
A | HOH278 |
B | ARG14 |
D | ASP125 |
D | ILE126 |
D | GLU127 |
site_id | BC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE TBR C 157 |
Chain | Residue |
B | SER124 |
B | ILE126 |
B | GLU127 |
B | HOH305 |
C | LYS39 |
C | ASP40 |
C | GLN42 |
C | HOH266 |
D | ARG14 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE TBR A 159 |
Chain | Residue |
A | LYS39 |
A | TBR158 |
A | HOH250 |
A | HOH278 |
B | SER151 |
D | MET1 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE TBR D 158 |
Chain | Residue |
A | LYS129 |
A | ZEA157 |
D | ASP75 |
D | SER78 |
D | GLU80 |
D | HOH248 |
site_id | BC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE TBR C 158 |
Chain | Residue |
C | GLU73 |
C | ASP75 |
C | SER78 |
C | GLU80 |
C | LYS134 |
C | SER138 |
C | HOH251 |
C | HOH257 |
C | HOH264 |
C | HOH265 |
C | HOH297 |
C | ILE37 |
site_id | BC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE EPE A 160 |
Chain | Residue |
A | ASP47 |
A | GLY49 |
A | PHE74 |
A | ASP75 |
A | GLU76 |
A | HOH187 |
A | HOH220 |
A | HOH264 |
B | THR133 |
B | HOH236 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16998071, ECO:0000269|PubMed:18453695, ECO:0007744|PDB:2FLH, ECO:0007744|PDB:3C0V |
Chain | Residue | Details |
A | LEU22 | |
D | LEU22 | |
D | GLN67 | |
D | GLU69 | |
A | GLN67 | |
A | GLU69 | |
B | LEU22 | |
B | GLN67 | |
B | GLU69 | |
C | LEU22 | |
C | GLN67 | |
C | GLU69 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25004979, ECO:0007744|PDB:4PSB |
Chain | Residue | Details |
A | THR139 | |
B | THR139 | |
C | THR139 | |
D | THR139 |