6TZ6
Crystal Structure of Candida Albicans Calcineurin A, Calcineurin B, FKBP12 and FK506 (Tacrolimus)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0033192 | molecular_function | calmodulin-dependent protein phosphatase activity |
| A | 0097720 | biological_process | calcineurin-mediated signaling |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0001228 | molecular_function | DNA-binding transcription activator activity, RNA polymerase II-specific |
| C | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| C | 0005527 | molecular_function | macrolide binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006325 | biological_process | chromatin organization |
| C | 0006366 | biological_process | transcription by RNA polymerase II |
| C | 0006457 | biological_process | protein folding |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0044183 | molecular_function | protein folding chaperone |
| C | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| C | 0062040 | cellular_component | fungal biofilm matrix |
| C | 0070651 | biological_process | nonfunctional rRNA decay |
| C | 0071466 | biological_process | cellular response to xenobiotic stimulus |
| C | 1901710 | biological_process | regulation of homoserine biosynthetic process |
| C | 1901711 | biological_process | negative regulation of homoserine biosynthetic process |
| C | 1903332 | biological_process | regulation of protein folding |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0033192 | molecular_function | calmodulin-dependent protein phosphatase activity |
| D | 0097720 | biological_process | calcineurin-mediated signaling |
| E | 0005509 | molecular_function | calcium ion binding |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0001228 | molecular_function | DNA-binding transcription activator activity, RNA polymerase II-specific |
| F | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| F | 0005527 | molecular_function | macrolide binding |
| F | 0005576 | cellular_component | extracellular region |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006325 | biological_process | chromatin organization |
| F | 0006366 | biological_process | transcription by RNA polymerase II |
| F | 0006457 | biological_process | protein folding |
| F | 0016853 | molecular_function | isomerase activity |
| F | 0044183 | molecular_function | protein folding chaperone |
| F | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| F | 0062040 | cellular_component | fungal biofilm matrix |
| F | 0070651 | biological_process | nonfunctional rRNA decay |
| F | 0071466 | biological_process | cellular response to xenobiotic stimulus |
| F | 1901710 | biological_process | regulation of homoserine biosynthetic process |
| F | 1901711 | biological_process | negative regulation of homoserine biosynthetic process |
| F | 1903332 | biological_process | regulation of protein folding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue PO4 A 501 |
| Chain | Residue |
| A | HIS141 |
| A | HOH604 |
| A | HOH607 |
| A | HOH654 |
| A | HOH707 |
| A | ASP167 |
| A | ARG171 |
| A | ASN199 |
| A | HIS200 |
| A | ARG303 |
| A | HIS330 |
| A | ZN502 |
| A | FE503 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue ZN A 502 |
| Chain | Residue |
| A | ASP167 |
| A | ASN199 |
| A | HIS248 |
| A | HIS330 |
| A | PO4501 |
| A | FE503 |
| A | HOH604 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue FE A 503 |
| Chain | Residue |
| A | ASP139 |
| A | HIS141 |
| A | ASP167 |
| A | PO4501 |
| A | ZN502 |
| A | HOH604 |
| A | HOH707 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | TYR85 |
| A | HIS92 |
| A | GLN93 |
| A | ASN188 |
| A | TYR189 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 200 |
| Chain | Residue |
| B | ASP102 |
| B | ASP104 |
| B | ASP106 |
| B | TYR108 |
| B | GLU113 |
| B | HOH306 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue CA B 201 |
| Chain | Residue |
| B | ASP143 |
| B | ASP145 |
| B | ASP147 |
| B | LYS149 |
| B | GLU154 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 202 |
| Chain | Residue |
| B | ASP65 |
| B | ASP67 |
| B | ASP69 |
| B | SER71 |
| B | ASP73 |
| B | GLU76 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | binding site for residue FK5 C 200 |
| Chain | Residue |
| A | TRP401 |
| A | SER402 |
| A | PRO404 |
| A | PHE405 |
| A | GLU408 |
| A | HOH609 |
| A | HOH682 |
| B | MET118 |
| B | MET121 |
| B | VAL122 |
| C | TYR30 |
| C | PHE40 |
| C | ASP41 |
| C | ARG46 |
| C | GLN58 |
| C | VAL59 |
| C | ILE60 |
| C | TRP63 |
| C | ALA96 |
| C | TYR97 |
| C | PHE114 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | binding site for residue PO4 D 501 |
| Chain | Residue |
| D | HIS141 |
| D | ASP167 |
| D | ARG171 |
| D | ASN199 |
| D | HIS200 |
| D | ARG303 |
| D | HIS330 |
| D | ZN502 |
| D | FE503 |
| D | HOH604 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue ZN D 502 |
| Chain | Residue |
| D | ASP167 |
| D | ASN199 |
| D | HIS248 |
| D | HIS330 |
| D | PO4501 |
| D | FE503 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue FE D 503 |
| Chain | Residue |
| D | ASP139 |
| D | HIS141 |
| D | ASP167 |
| D | PO4501 |
| D | ZN502 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 D 504 |
| Chain | Residue |
| D | HIS204 |
| D | LEU205 |
| D | HOH607 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 505 |
| Chain | Residue |
| A | ARG268 |
| D | LYS115 |
| D | HOH639 |
| D | HOH665 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue CA E 200 |
| Chain | Residue |
| E | ASP104 |
| E | ASP106 |
| E | TYR108 |
| E | GLU113 |
| E | HOH304 |
| E | ASP102 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue CA E 201 |
| Chain | Residue |
| E | ASP143 |
| E | ASP145 |
| E | ASP147 |
| E | LYS149 |
| E | GLU154 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue CA E 202 |
| Chain | Residue |
| E | ASP65 |
| E | ASP67 |
| E | ASP69 |
| E | SER71 |
| E | GLU76 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue CA E 203 |
| Chain | Residue |
| E | ASP35 |
| E | SER37 |
| E | GLN39 |
| E | GLU44 |
| E | HOH302 |
| site_id | AD9 |
| Number of Residues | 18 |
| Details | binding site for residue FK5 F 200 |
| Chain | Residue |
| D | TRP401 |
| D | PRO404 |
| D | PHE405 |
| D | GLU408 |
| E | MET121 |
| E | ASN125 |
| F | TYR30 |
| F | PHE40 |
| F | ASP41 |
| F | PHE50 |
| F | GLN58 |
| F | VAL59 |
| F | ILE60 |
| F | TRP63 |
| F | ALA96 |
| F | TYR97 |
| F | PHE114 |
| F | HOH303 |
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DKDGSGQIDkqEF |
| Chain | Residue | Details |
| B | ASP33-PHE45 | |
| B | ASP65-PHE77 | |
| B | ASP102-LEU114 | |
| B | ASP143-PHE155 |
| site_id | PS00125 |
| Number of Residues | 6 |
| Details | SER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE |
| Chain | Residue | Details |
| A | LEU196-GLU201 |
