4MFH
Crystal Structure of M121G Azurin
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU A 201 |
| Chain | Residue |
| A | GLY45 |
| A | HIS46 |
| A | CYS112 |
| A | HIS117 |
| A | HOH304 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU A 202 |
| Chain | Residue |
| B | HOH364 |
| A | HIS83 |
| A | TRS203 |
| B | ALA1 |
| B | HOH348 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TRS A 203 |
| Chain | Residue |
| A | LYS74 |
| A | ASP76 |
| A | ASP77 |
| A | VAL80 |
| A | HIS83 |
| A | CU202 |
| A | HOH380 |
| A | HOH386 |
| A | HOH393 |
| B | ALA1 |
| B | CYS3 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU B 201 |
| Chain | Residue |
| B | GLY45 |
| B | HIS46 |
| B | CYS112 |
| B | HIS117 |
| B | HOH312 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 202 |
| Chain | Residue |
| B | HIS83 |
| B | TRS203 |
| B | HOH395 |
| C | ALA1 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TRS B 203 |
| Chain | Residue |
| B | LYS74 |
| B | ASP76 |
| B | ASP77 |
| B | VAL80 |
| B | HIS83 |
| B | CU202 |
| B | HOH375 |
| C | ALA1 |
| C | CYS3 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU C 201 |
| Chain | Residue |
| C | GLY45 |
| C | HIS46 |
| C | CYS112 |
| C | HIS117 |
| C | HOH398 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU C 202 |
| Chain | Residue |
| A | ALA1 |
| A | HOH325 |
| A | HOH329 |
| C | HIS83 |
| C | TRS203 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TRS C 203 |
| Chain | Residue |
| A | ALA1 |
| A | CYS3 |
| C | LYS74 |
| C | ASP76 |
| C | ASP77 |
| C | HIS83 |
| C | CU202 |
| C | HOH309 |
| C | HOH350 |
| C | HOH383 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 381 |
| Details | Domain: {"description":"Plastocyanin-like"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"1420141","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {} |
| Chain | Residue | Details |
