2IWE
Structure of a cavity mutant (H117G) of Pseudomonas aeruginosa azurin
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 |
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 |
G | 0005507 | molecular_function | copper ion binding |
G | 0005515 | molecular_function | protein binding |
G | 0008270 | molecular_function | zinc ion binding |
G | 0009055 | molecular_function | electron transfer activity |
G | 0042597 | cellular_component | periplasmic space |
G | 0042802 | molecular_function | identical protein binding |
G | 0046872 | molecular_function | metal ion binding |
G | 0046914 | molecular_function | transition metal ion binding |
J | 0005507 | molecular_function | copper ion binding |
J | 0005515 | molecular_function | protein binding |
J | 0008270 | molecular_function | zinc ion binding |
J | 0009055 | molecular_function | electron transfer activity |
J | 0042597 | cellular_component | periplasmic space |
J | 0042802 | molecular_function | identical protein binding |
J | 0046872 | molecular_function | metal ion binding |
J | 0046914 | molecular_function | transition metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 1129 |
Chain | Residue |
A | GLY45 |
A | HIS46 |
A | CYS112 |
A | MET121 |
A | 2IH1001 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN D 1129 |
Chain | Residue |
D | 2IH1001 |
D | GLY45 |
D | HIS46 |
D | CYS112 |
D | MET121 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN G 1129 |
Chain | Residue |
D | 2IH1001 |
G | GLY45 |
G | HIS46 |
G | CYS112 |
G | PHE114 |
G | MET121 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN J 1129 |
Chain | Residue |
A | 2IH1001 |
J | GLY45 |
J | HIS46 |
J | CYS112 |
J | PHE114 |
J | MET121 |
site_id | AC5 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE 2IH A 1001 |
Chain | Residue |
A | MET13 |
A | VAL43 |
A | MET44 |
A | GLY45 |
A | HIS46 |
A | CYS112 |
A | PHE114 |
A | PRO115 |
A | GLY116 |
A | MET121 |
A | ZN1129 |
J | VAL43 |
J | MET44 |
J | GLY45 |
J | HIS46 |
J | CYS112 |
J | PHE114 |
J | GLY116 |
J | ZN1129 |
site_id | AC6 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE 2IH D 1001 |
Chain | Residue |
D | VAL43 |
D | MET44 |
D | GLY45 |
D | HIS46 |
D | CYS112 |
D | PHE114 |
D | GLY116 |
D | ZN1129 |
G | MET13 |
G | VAL43 |
G | MET44 |
G | GLY45 |
G | HIS46 |
G | PHE114 |
G | PRO115 |
G | GLY116 |
G | MET121 |
G | ZN1129 |
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 | |
J | HIS46 | |
J | CYS112 | |
J | GLY117 | |
A | CYS112 | |
A | GLY117 | |
D | HIS46 | |
D | CYS112 | |
D | GLY117 | |
G | HIS46 | |
G | CYS112 | |
G | GLY117 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | MET121 | |
D | MET121 | |
G | MET121 | |
J | MET121 |