1QHB
VANADIUM BROMOPEROXIDASE FROM RED ALGA CORALLINA OFFICINALIS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0019806 | molecular_function | bromide peroxidase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0019806 | molecular_function | bromide peroxidase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
| C | 0004601 | molecular_function | peroxidase activity |
| C | 0019806 | molecular_function | bromide peroxidase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0098869 | biological_process | cellular oxidant detoxification |
| D | 0004601 | molecular_function | peroxidase activity |
| D | 0019806 | molecular_function | bromide peroxidase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0098869 | biological_process | cellular oxidant detoxification |
| E | 0004601 | molecular_function | peroxidase activity |
| E | 0019806 | molecular_function | bromide peroxidase activity |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0098869 | biological_process | cellular oxidant detoxification |
| F | 0004601 | molecular_function | peroxidase activity |
| F | 0019806 | molecular_function | bromide peroxidase activity |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 3000 |
| Chain | Residue |
| A | LYS398 |
| A | ARG406 |
| A | PRO476 |
| A | HIS478 |
| A | SER483 |
| A | GLY484 |
| A | HIS485 |
| A | ARG545 |
| A | HIS551 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 3001 |
| Chain | Residue |
| A | PHE359 |
| A | GLN361 |
| A | ASP363 |
| A | ASP366 |
| A | GLN368 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 3002 |
| Chain | Residue |
| B | LYS398 |
| B | ARG406 |
| B | PRO476 |
| B | HIS478 |
| B | SER483 |
| B | GLY484 |
| B | HIS485 |
| B | ARG545 |
| B | HIS551 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 3003 |
| Chain | Residue |
| B | PHE359 |
| B | GLN361 |
| B | ASP363 |
| B | ASP366 |
| B | GLN368 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 C 3004 |
| Chain | Residue |
| C | GLY484 |
| C | HIS485 |
| C | ARG545 |
| C | HIS551 |
| C | LYS398 |
| C | ARG406 |
| C | PRO476 |
| C | HIS478 |
| C | SER483 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA C 3005 |
| Chain | Residue |
| C | PHE359 |
| C | GLN361 |
| C | ASP363 |
| C | ASP366 |
| C | GLN368 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 D 3006 |
| Chain | Residue |
| D | LYS398 |
| D | ARG406 |
| D | PRO476 |
| D | HIS478 |
| D | SER483 |
| D | GLY484 |
| D | HIS485 |
| D | ARG545 |
| D | HIS551 |
| D | HOH3267 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA D 3007 |
| Chain | Residue |
| D | PHE359 |
| D | GLN361 |
| D | ASP363 |
| D | ASP366 |
| D | GLN368 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 E 3008 |
| Chain | Residue |
| E | LYS398 |
| E | ARG406 |
| E | PRO476 |
| E | HIS478 |
| E | SER483 |
| E | GLY484 |
| E | HIS485 |
| E | ARG545 |
| E | HIS551 |
| E | HOH3334 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA E 3009 |
| Chain | Residue |
| E | PHE359 |
| E | GLN361 |
| E | ASP363 |
| E | ASP366 |
| E | GLN368 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 F 3010 |
| Chain | Residue |
| F | LYS398 |
| F | ARG406 |
| F | PRO476 |
| F | HIS478 |
| F | SER483 |
| F | GLY484 |
| F | HIS485 |
| F | ARG545 |
| F | HIS551 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA F 3011 |
| Chain | Residue |
| F | PHE359 |
| F | GLN361 |
| F | ASP363 |
| F | ASP366 |
| F | GLN368 |
| site_id | CAA |
| Number of Residues | 4 |
| Details | CALCIUM BINDING SITE IN SUBUNIT A |
| Chain | Residue |
| A | PHE359 |
| A | GLN361 |
| A | ASP363 |
| A | ASP366 |
| site_id | CAB |
| Number of Residues | 4 |
| Details | CALCIUM BINDING SITE IN SUBUNIT B |
| Chain | Residue |
| E | PHE359 |
| E | GLN361 |
| E | ASP363 |
| E | ASP366 |
| site_id | CAC |
| Number of Residues | 4 |
| Details | CALCIUM BINDING SITE IN SUBUNIT C |
| Chain | Residue |
| E | GLN361 |
| E | ASP363 |
| E | ASP366 |
| E | PHE359 |
| site_id | CAD |
| Number of Residues | 4 |
| Details | CALCIUM BINDING SITE IN SUBUNIT D |
| Chain | Residue |
| D | PHE359 |
| D | GLN361 |
| D | ASP363 |
| D | ASP366 |
| site_id | CAE |
| Number of Residues | 4 |
| Details | CALCIUM BINDING SITE IN SUBUNIT E |
| Chain | Residue |
| E | PHE359 |
| E | GLN361 |
| E | ASP363 |
| E | ASP366 |
| site_id | CAF |
| Number of Residues | 4 |
| Details | CALCIUM BINDING SITE IN SUBUNIT F |
| Chain | Residue |
| F | PHE359 |
| F | GLN361 |
| F | ASP363 |
| F | ASP366 |
| site_id | VAA |
| Number of Residues | 7 |
| Details | VANADATE BINDING SITE IN SUBUNIT A |
| Chain | Residue |
| A | LYS398 |
| A | ARG406 |
| A | SER483 |
| A | GLY484 |
| A | HIS485 |
| A | ARG545 |
| A | HIS551 |
| site_id | VAB |
| Number of Residues | 7 |
| Details | VANADATE BINDING SITE IN SUBUNIT B |
| Chain | Residue |
| E | LYS398 |
| E | ARG406 |
| E | SER483 |
| E | GLY484 |
| E | HIS485 |
| E | ARG545 |
| E | HIS551 |
| site_id | VAC |
| Number of Residues | 7 |
| Details | VANADATE BINDING SITE IN SUBUNIT C |
| Chain | Residue |
| E | LYS398 |
| E | ARG406 |
| E | SER483 |
| E | GLY484 |
| E | HIS485 |
| E | ARG545 |
| E | HIS551 |
| site_id | VAD |
| Number of Residues | 7 |
| Details | VANADATE BINDING SITE IN SUBUNIT D |
| Chain | Residue |
| D | LYS398 |
| D | ARG406 |
| D | SER483 |
| D | GLY484 |
| D | HIS485 |
| D | ARG545 |
| D | HIS551 |
| site_id | VAE |
| Number of Residues | 7 |
| Details | VANADATE BINDING SITE IN SUBUNIT E |
| Chain | Residue |
| E | LYS398 |
| E | ARG406 |
| E | SER483 |
| E | GLY484 |
| E | HIS485 |
| E | ARG545 |
| E | HIS551 |
| site_id | VAF |
| Number of Residues | 7 |
| Details | VANADATE BINDING SITE IN SUBUNIT F |
| Chain | Residue |
| F | LYS398 |
| F | ARG406 |
| F | SER483 |
| F | GLY484 |
| F | HIS485 |
| F | ARG545 |
| F | HIS551 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| D | SER480 | |
| D | VAL487 | |
| E | SER480 | |
| E | VAL487 | |
| F | SER480 | |
| F | VAL487 | |
| A | SER480 | |
| A | VAL487 | |
| B | SER480 | |
| B | VAL487 | |
| C | SER480 | |
| C | VAL487 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 30 |
| Details | BINDING: BINDING => ECO:0007744|PDB:1QHB |
| Chain | Residue | Details |
| C | LEU365 | |
| C | GLN368 | |
| C | VAL370 | |
| D | GLN361 | |
| D | ASP363 | |
| D | LEU365 | |
| D | GLN368 | |
| D | VAL370 | |
| E | GLN361 | |
| E | ASP363 | |
| E | LEU365 | |
| E | GLN368 | |
| E | VAL370 | |
| F | GLN361 | |
| F | ASP363 | |
| F | LEU365 | |
| F | GLN368 | |
| F | VAL370 | |
| A | GLN361 | |
| A | ASP363 | |
| A | LEU365 | |
| A | GLN368 | |
| A | VAL370 | |
| B | GLN361 | |
| B | ASP363 | |
| B | LEU365 | |
| B | GLN368 | |
| B | VAL370 | |
| C | GLN361 | |
| C | ASP363 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 42 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P81701 |
| Chain | Residue | Details |
| A | ASN400 | |
| A | GLU408 | |
| D | ALA486 | |
| D | VAL487 | |
| D | MET547 | |
| D | PHE553 | |
| E | ASN400 | |
| E | GLU408 | |
| E | HIS485 | |
| E | ALA486 | |
| E | VAL487 | |
| E | MET547 | |
| E | PHE553 | |
| F | ASN400 | |
| F | GLU408 | |
| F | HIS485 | |
| F | ALA486 | |
| F | VAL487 | |
| F | MET547 | |
| F | PHE553 | |
| A | HIS485 | |
| A | ALA486 | |
| A | VAL487 | |
| A | MET547 | |
| A | PHE553 | |
| B | ASN400 | |
| B | GLU408 | |
| B | HIS485 | |
| B | ALA486 | |
| B | VAL487 | |
| B | MET547 | |
| B | PHE553 | |
| C | ASN400 | |
| C | GLU408 | |
| C | HIS485 | |
| C | ALA486 | |
| C | VAL487 | |
| C | MET547 | |
| C | PHE553 | |
| D | ASN400 | |
| D | GLU408 | |
| D | HIS485 |
