4BWW
Crystal structure of spin labelled azurin T21R1.
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 B 1129 |
| Chain | Residue |
| B | GLY45 |
| B | HIS46 |
| B | CYS112 |
| B | HIS117 |
| B | MET121 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU C 1129 |
| Chain | Residue |
| C | MET121 |
| C | GLY45 |
| C | HIS46 |
| C | CYS112 |
| C | HIS117 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CU A 1129 |
| Chain | Residue |
| A | GLY45 |
| A | HIS46 |
| A | CYS112 |
| A | PHE114 |
| A | HIS117 |
| A | MET121 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU D 1129 |
| Chain | Residue |
| D | GLY45 |
| D | HIS46 |
| D | CYS112 |
| D | HIS117 |
| D | MET121 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE NO3 B 1130 |
| Chain | Residue |
| A | ASN18 |
| A | HOH2036 |
| B | VAL60 |
| B | GLY116 |
| B | HIS117 |
| B | SER118 |
| B | ALA119 |
| B | GOL1137 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1130 |
| Chain | Residue |
| A | LYS74 |
| A | ASP77 |
| A | SER78 |
| A | ARG79 |
| A | HOH2088 |
| A | HOH2101 |
| A | HOH2108 |
| C | HOH2035 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 1130 |
| Chain | Residue |
| C | ASP76 |
| C | HIS83 |
| C | HOH2081 |
| C | HOH2086 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 1131 |
| Chain | Residue |
| A | GLN57 |
| A | HOH2081 |
| B | PRO40 |
| B | ASN42 |
| B | VAL43 |
| C | GLY37 |
| C | ASN38 |
| C | HOH2060 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL D 1130 |
| Chain | Residue |
| A | ASN42 |
| A | LEU68 |
| A | HOH2073 |
| C | ALA119 |
| C | HOH2120 |
| D | SER66 |
| D | GLY67 |
| D | LEU68 |
| D | ASP69 |
| D | HOH2093 |
| D | HOH2094 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1131 |
| Chain | Residue |
| B | PRO75 |
| B | ASP76 |
| B | HIS83 |
| B | HOH2071 |
| B | HOH2073 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NO3 A 1131 |
| Chain | Residue |
| A | LYS122 |
| A | HOH2152 |
| A | HOH2153 |
| A | HOH2154 |
| A | HOH2155 |
| B | LEU68 |
| B | TYR72 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1132 |
| Chain | Residue |
| B | ALA1 |
| B | SER4 |
| B | ILE20 |
| B | R1A21 |
| B | SO41134 |
| D | ASN18 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE NO3 D 1131 |
| Chain | Residue |
| C | ASN18 |
| C | ALA19 |
| C | HOH2039 |
| D | VAL60 |
| D | GLY116 |
| D | HIS117 |
| D | SER118 |
| D | ALA119 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1133 |
| Chain | Residue |
| A | HOH2054 |
| B | ALA1 |
| B | GLU2 |
| B | CYS3 |
| B | SER4 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1134 |
| Chain | Residue |
| B | GOL1132 |
| B | HOH2026 |
| B | HOH2027 |
| B | HOH2117 |
| D | THR17 |
| D | ASN18 |
| D | ALA19 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1132 |
| Chain | Residue |
| D | GLU2 |
| D | CYS3 |
| D | SER4 |
| D | ALA1 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1132 |
| Chain | Residue |
| B | ASN38 |
| C | LYS41 |
| C | HOH2062 |
| C | HOH2063 |
| C | HOH2097 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1133 |
| Chain | Residue |
| D | GLU2 |
| D | CYS3 |
| D | SER25 |
| D | CYS26 |
| site_id | CC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 1135 |
| Chain | Residue |
| A | ALA119 |
| A | HOH2155 |
| B | SER66 |
| B | GLY67 |
| B | LEU68 |
| B | ASP69 |
| B | HOH2118 |
| C | ASN42 |
| C | LEU68 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NO3 B 1136 |
| Chain | Residue |
| B | ASN10 |
| B | ASP11 |
| B | GLN12 |
| B | PRO36 |
| B | GLY37 |
| site_id | CC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 1137 |
| Chain | Residue |
| A | ASN18 |
| B | VAL60 |
| B | MET64 |
| B | THR113 |
| B | PRO115 |
| B | GLY116 |
| B | NO31130 |
| B | HOH2108 |
| site_id | CC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE NO3 C 1133 |
| Chain | Residue |
| A | GLY58 |
| A | HOH2087 |
| C | ASN10 |
| C | ASP11 |
| C | GLN12 |
| C | PRO36 |
| C | GLY37 |
| C | HOH2031 |
| C | HOH2059 |
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 site: {"evidences":[{"source":"PubMed","id":"1420141","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| Chain | Residue | Details |
