1YE9
Crystal structure of proteolytically truncated catalase HPII from E. coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004096 | molecular_function | catalase activity |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0020037 | molecular_function | heme binding |
| B | 0004096 | molecular_function | catalase activity |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0020037 | molecular_function | heme binding |
| C | 0004096 | molecular_function | catalase activity |
| C | 0006979 | biological_process | response to oxidative stress |
| C | 0020037 | molecular_function | heme binding |
| D | 0004096 | molecular_function | catalase activity |
| D | 0006979 | biological_process | response to oxidative stress |
| D | 0020037 | molecular_function | heme binding |
| E | 0004096 | molecular_function | catalase activity |
| E | 0006979 | biological_process | response to oxidative stress |
| E | 0020037 | molecular_function | heme binding |
| F | 0004096 | molecular_function | catalase activity |
| F | 0006979 | biological_process | response to oxidative stress |
| F | 0020037 | molecular_function | heme binding |
| G | 0004096 | molecular_function | catalase activity |
| G | 0006979 | biological_process | response to oxidative stress |
| G | 0020037 | molecular_function | heme binding |
| H | 0004096 | molecular_function | catalase activity |
| H | 0006979 | biological_process | response to oxidative stress |
| H | 0020037 | molecular_function | heme binding |
| I | 0004096 | molecular_function | catalase activity |
| I | 0006979 | biological_process | response to oxidative stress |
| I | 0020037 | molecular_function | heme binding |
| J | 0004096 | molecular_function | catalase activity |
| J | 0006979 | biological_process | response to oxidative stress |
| J | 0020037 | molecular_function | heme binding |
| K | 0004096 | molecular_function | catalase activity |
| K | 0006979 | biological_process | response to oxidative stress |
| K | 0020037 | molecular_function | heme binding |
| L | 0004096 | molecular_function | catalase activity |
| L | 0006979 | biological_process | response to oxidative stress |
| L | 0020037 | molecular_function | heme binding |
| M | 0004096 | molecular_function | catalase activity |
| M | 0006979 | biological_process | response to oxidative stress |
| M | 0020037 | molecular_function | heme binding |
| N | 0004096 | molecular_function | catalase activity |
| N | 0006979 | biological_process | response to oxidative stress |
| N | 0020037 | molecular_function | heme binding |
| O | 0004096 | molecular_function | catalase activity |
| O | 0006979 | biological_process | response to oxidative stress |
| O | 0020037 | molecular_function | heme binding |
| P | 0004096 | molecular_function | catalase activity |
| P | 0006979 | biological_process | response to oxidative stress |
| P | 0020037 | molecular_function | heme binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HDD E 760 |
| Chain | Residue |
| A | ARG125 |
| A | PHE214 |
| A | ILE274 |
| A | HOH303 |
| D | PHE117 |
| E | HOH137 |
| E | PHE391 |
| E | LEU407 |
| E | ARG411 |
| E | SER414 |
| E | TYR415 |
| A | VAL127 |
| E | GLN419 |
| A | HIS128 |
| A | ARG165 |
| A | GLY184 |
| A | VAL199 |
| A | GLY200 |
| A | ASN201 |
| A | PHE206 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HDD F 760 |
| Chain | Residue |
| B | ARG125 |
| B | ILE126 |
| B | VAL127 |
| B | HIS128 |
| B | ARG165 |
| B | GLY184 |
| B | VAL199 |
| B | GLY200 |
| B | ASN201 |
| B | PHE206 |
| B | PHE214 |
| B | ILE274 |
| F | PHE391 |
| F | LEU407 |
| F | ARG411 |
| F | SER414 |
| F | TYR415 |
| F | THR418 |
| F | GLN419 |
| F | ARG422 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HDD G 760 |
| Chain | Residue |
| B | PHE117 |
| C | ARG125 |
| C | ILE126 |
| C | VAL127 |
| C | HIS128 |
| C | ARG165 |
| C | GLY184 |
| C | VAL199 |
| C | GLY200 |
| C | ASN201 |
| C | PHE206 |
| C | PHE214 |
| C | ILE274 |
| C | HIS275 |
| G | PHE391 |
| G | LEU407 |
| G | ARG411 |
| G | SER414 |
| G | TYR415 |
| G | THR418 |
| G | GLN419 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HDD H 760 |
| Chain | Residue |
| D | ARG125 |
| D | ILE126 |
| D | VAL127 |
| D | HIS128 |
| D | ARG165 |
| D | GLY184 |
| D | VAL199 |
| D | GLY200 |
| D | ASN201 |
| D | PHE206 |
| D | PHE214 |
| H | PHE391 |
| H | LEU407 |
| H | ARG411 |
| H | SER414 |
| H | TYR415 |
| H | THR418 |
| H | GLN419 |
| H | ARG422 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HDD M 760 |
| Chain | Residue |
| I | ARG125 |
| I | ILE126 |
| I | VAL127 |
| I | HIS128 |
| I | ARG165 |
| I | GLY184 |
| I | VAL199 |
| I | GLY200 |
| I | ASN201 |
| I | PHE214 |
| I | HIS275 |
| M | PHE391 |
| M | LEU407 |
| M | ARG411 |
| M | SER414 |
| M | TYR415 |
| M | THR418 |
| M | GLN419 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HDD N 760 |
| Chain | Residue |
| J | VAL127 |
| J | HIS128 |
| J | ARG165 |
| J | GLY184 |
| J | VAL199 |
| J | GLY200 |
| J | ASN201 |
| J | PHE206 |
| J | PHE214 |
| J | ILE274 |
| K | PHE117 |
| N | PHE391 |
| N | LEU407 |
| N | ARG411 |
| N | SER414 |
| N | TYR415 |
| N | GLN419 |
| J | ARG125 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HDD O 760 |
| Chain | Residue |
| K | ARG125 |
| K | VAL127 |
| K | HIS128 |
| K | ARG165 |
| K | GLY184 |
| K | VAL199 |
| K | GLY200 |
| K | ASN201 |
| K | PHE206 |
| K | PHE214 |
| K | HIS275 |
| O | PHE391 |
| O | LEU407 |
| O | ARG411 |
| O | SER414 |
| O | TYR415 |
| O | THR418 |
| O | GLN419 |
| O | ARG422 |
| O | HOH761 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HDD P 760 |
| Chain | Residue |
| L | ARG125 |
| L | ILE126 |
| L | VAL127 |
| L | HIS128 |
| L | ARG165 |
| L | GLY184 |
| L | ALA186 |
| L | VAL199 |
| L | GLY200 |
| L | ASN201 |
| L | PHE206 |
| L | PHE214 |
| L | ILE274 |
| P | PHE391 |
| P | ARG411 |
| P | SER414 |
| P | TYR415 |
| P | THR418 |
| P | GLN419 |
| P | ARG422 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| E | TYR415 | |
| I | ASN201 | |
| J | HIS128 | |
| J | ASN201 | |
| K | HIS128 | |
| K | ASN201 | |
| L | HIS128 | |
| L | ASN201 | |
| F | TYR415 | |
| G | TYR415 | |
| H | TYR415 | |
| M | TYR415 | |
| N | TYR415 | |
| O | TYR415 | |
| P | TYR415 | |
| I | HIS128 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | CROSSLNK: 3'-histidyl-3-tyrosine (His-Tyr) |
| Chain | Residue | Details |
| E | HIS392 | |
| M | TYR415 | |
| N | HIS392 | |
| N | TYR415 | |
| O | HIS392 | |
| O | TYR415 | |
| P | HIS392 | |
| P | TYR415 | |
| E | TYR415 | |
| F | HIS392 | |
| F | TYR415 | |
| G | HIS392 | |
| G | TYR415 | |
| H | HIS392 | |
| H | TYR415 | |
| M | HIS392 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1iph |
| Chain | Residue | Details |
| A | ASN201 | |
| A | SER167 | |
| A | HIS128 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1iph |
| Chain | Residue | Details |
| B | ASN201 | |
| B | SER167 | |
| B | HIS128 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1iph |
| Chain | Residue | Details |
| C | ASN201 | |
| C | SER167 | |
| C | HIS128 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1iph |
| Chain | Residue | Details |
| D | ASN201 | |
| D | SER167 | |
| D | HIS128 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1iph |
| Chain | Residue | Details |
| I | ASN201 | |
| I | SER167 | |
| I | HIS128 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1iph |
| Chain | Residue | Details |
| J | ASN201 | |
| J | SER167 | |
| J | HIS128 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1iph |
| Chain | Residue | Details |
| K | ASN201 | |
| K | SER167 | |
| K | HIS128 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1iph |
| Chain | Residue | Details |
| L | ASN201 | |
| L | SER167 | |
| L | HIS128 |
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 573 |
| Chain | Residue | Details |
| E | HIS392 | proton shuttle (general acid/base) |
| A | ASN201 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 1 |
| Details | M-CSA 573 |
| Chain | Residue | Details |
| F | HIS392 | proton shuttle (general acid/base) |
| B | ASN201 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 1 |
| Details | M-CSA 573 |
| Chain | Residue | Details |
| G | HIS392 | proton shuttle (general acid/base) |
| C | ASN201 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 1 |
| Details | M-CSA 573 |
| Chain | Residue | Details |
| H | HIS392 | proton shuttle (general acid/base) |
| D | ASN201 | electrostatic stabiliser |
| site_id | MCSA5 |
| Number of Residues | 1 |
| Details | M-CSA 573 |
| Chain | Residue | Details |
| M | HIS392 | proton shuttle (general acid/base) |
| I | ASN201 | electrostatic stabiliser |
| site_id | MCSA6 |
| Number of Residues | 1 |
| Details | M-CSA 573 |
| Chain | Residue | Details |
| N | HIS392 | proton shuttle (general acid/base) |
| J | ASN201 | electrostatic stabiliser |
| site_id | MCSA7 |
| Number of Residues | 1 |
| Details | M-CSA 573 |
| Chain | Residue | Details |
| O | HIS392 | proton shuttle (general acid/base) |
| K | ASN201 | electrostatic stabiliser |
| site_id | MCSA8 |
| Number of Residues | 1 |
| Details | M-CSA 573 |
| Chain | Residue | Details |
| P | HIS392 | proton shuttle (general acid/base) |
| L | ASN201 | electrostatic stabiliser |
