4HZ1
Crystal Structure of Pseudomonas aeruginosa azurin with iron(II) at the copper-binding site.
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 | 2 |
Details | BINDING SITE FOR RESIDUE ACT A 201 |
Chain | Residue |
A | THR17 |
A | ASN18 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A 202 |
Chain | Residue |
A | MET109 |
A | LYS122 |
A | THR124 |
D | GLN12 |
D | GLN14 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT A 203 |
Chain | Residue |
D | GLN12 |
A | LYS122 |
B | SER118 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE2 B 201 |
Chain | Residue |
B | GLY45 |
B | HIS46 |
B | CYS112 |
B | HIS117 |
B | MET121 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT B 202 |
Chain | Residue |
B | ASN10 |
B | ASP11 |
B | GLN12 |
B | PRO36 |
B | GLY37 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE2 C 201 |
Chain | Residue |
C | GLY45 |
C | HIS46 |
C | CYS112 |
C | PHE114 |
C | HIS117 |
C | MET121 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT C 202 |
Chain | Residue |
C | GLY116 |
C | SER118 |
D | LYS122 |
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 |