4JKN
Mercury Metallated Pseudomonas aeruginosa Azurin at 1.54 A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005515 | molecular_function | protein binding |
| 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 | 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 | 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 | 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 HG A 201 |
| Chain | Residue |
| A | GLY45 |
| A | HIS46 |
| A | CYS112 |
| A | HIS117 |
| A | MET121 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE HG A 202 |
| Chain | Residue |
| A | HOH409 |
| B | MET56 |
| B | HOH362 |
| A | MET56 |
| A | HOH305 |
| A | HOH340 |
| A | HOH347 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NO3 A 203 |
| Chain | Residue |
| A | CYS26 |
| A | LYS27 |
| A | GLN28 |
| B | PRO40 |
| B | ASN42 |
| B | HOH304 |
| D | LEU68 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NO3 A 204 |
| Chain | Residue |
| A | MET109 |
| A | LYS122 |
| A | THR124 |
| A | HOH346 |
| A | HOH399 |
| D | GLN14 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HG B 201 |
| Chain | Residue |
| B | GLY45 |
| B | HIS46 |
| B | CYS112 |
| B | HIS117 |
| B | MET121 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NO3 B 202 |
| Chain | Residue |
| B | SER94 |
| B | VAL95 |
| B | THR96 |
| C | LYS41 |
| C | ASN42 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HG C 201 |
| Chain | Residue |
| C | GLY45 |
| C | HIS46 |
| C | CYS112 |
| C | HIS117 |
| C | MET121 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HG D 201 |
| Chain | Residue |
| D | GLY45 |
| D | HIS46 |
| D | CYS112 |
| D | HIS117 |
| D | MET121 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE NO3 D 202 |
| Chain | Residue |
| D | GLU2 |
| D | CYS3 |
| D | SER4 |
| D | THR21 |
| D | VAL22 |
| D | ASP23 |
| D | CYS26 |
| D | PHE29 |
| D | HOH378 |
| D | HOH385 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NO3 D 203 |
| Chain | Residue |
| D | THR96 |
| D | PHE97 |
| D | ASP98 |
| D | LYS101 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NO3 D 204 |
| Chain | Residue |
| D | PRO75 |
| D | ASP76 |
| D | HIS83 |
| D | HOH330 |
| D | HOH332 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NO3 D 205 |
| Chain | Residue |
| A | GLN12 |
| A | GLN14 |
| A | HOH327 |
| D | MET109 |
| D | LYS122 |
| D | THR124 |
| D | HOH376 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 D 206 |
| Chain | Residue |
| A | THR96 |
| A | PHE97 |
| A | ASP98 |
| A | LYS101 |
| D | LYS41 |
| D | HOH371 |
| D | HOH397 |
| D | HOH408 |
Functional Information from PROSITE/UniProt
| site_id | PS00196 |
| Number of Residues | 17 |
| Details | COPPER_BLUE Type-1 copper (blue) proteins signature. GeqYmFFCtfPgHsal.M |
| Chain | Residue | Details |
| A | GLY105-MET121 |
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 | HIS117 | |
| A | CYS112 | |
| A | HIS117 | |
| B | HIS46 | |
| B | CYS112 | |
| B | HIS117 | |
| C | HIS46 | |
| C | CYS112 | |
| C | HIS117 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | MET121 | |
| B | MET121 | |
| C | MET121 | |
| D | MET121 |
