2FTA
Structure of Cu(II)azurin with the metal-binding loop sequence "CTFPGHSALM" replaced with "CTPHPFM"
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046914 | molecular_function | transition metal ion binding |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0046914 | molecular_function | transition metal ion binding |
| C | 0005507 | molecular_function | copper ion binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0046914 | molecular_function | transition metal ion binding |
| D | 0005507 | molecular_function | copper ion binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0046914 | molecular_function | transition metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU A 126 |
| Chain | Residue |
| A | GLY45 |
| A | HIS46 |
| A | CYS112 |
| A | HIS115 |
| A | MET118 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU B 126 |
| Chain | Residue |
| B | MET118 |
| B | GLY45 |
| B | HIS46 |
| B | CYS112 |
| B | HIS115 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU C 126 |
| Chain | Residue |
| C | GLY45 |
| C | HIS46 |
| C | CYS112 |
| C | HIS115 |
| C | MET118 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU D 126 |
| Chain | Residue |
| D | GLY45 |
| D | HIS46 |
| D | CYS112 |
| D | HIS115 |
| D | MET118 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 2PE A 501 |
| Chain | Residue |
| A | PRO116 |
| A | PHE117 |
| A | LYS119 |
| A | EOH502 |
| A | PEG504 |
| A | HOH562 |
| A | HOH612 |
| A | HOH614 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 2PE D 505 |
| Chain | Residue |
| A | GLN107 |
| D | MET109 |
| D | PHE117 |
| D | LYS119 |
| D | GLY120 |
| D | HOH578 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EOH A 502 |
| Chain | Residue |
| A | GLN57 |
| A | 2PE501 |
| A | PEG504 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EOH A 503 |
| Chain | Residue |
| A | ASN18 |
| A | LYS119 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EOH A 506 |
| Chain | Residue |
| A | LYS74 |
| A | HOH605 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG A 504 |
| Chain | Residue |
| A | LYS119 |
| A | 2PE501 |
| A | EOH502 |
| A | HOH515 |
Functional Information from PROSITE/UniProt
| site_id | PS00196 |
| Number of Residues | 14 |
| Details | COPPER_BLUE Type-1 copper (blue) proteins signature. GeqYmFFCt.P.Hpf..M |
| Chain | Residue | Details |
| A | GLY105-MET118 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:1420141 |
| Chain | Residue | Details |
| A | HIS46 | |
| D | HIS46 | |
| D | CYS112 | |
| D | PHE117 | |
| A | CYS112 | |
| A | PHE117 | |
| B | HIS46 | |
| B | CYS112 | |
| B | PHE117 | |
| C | HIS46 | |
| C | CYS112 | |
| C | PHE117 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | THR121 | |
| B | THR121 | |
| C | THR121 | |
| D | THR121 |
