1SZZ
Crystal structure of peptide deformylase from Leptospira Interrogans complexed with inhibitor actinonin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006412 | biological_process | translation |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042586 | molecular_function | peptide deformylase activity |
| A | 0043686 | biological_process | co-translational protein modification |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0006412 | biological_process | translation |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0042586 | molecular_function | peptide deformylase activity |
| B | 0043686 | biological_process | co-translational protein modification |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0006412 | biological_process | translation |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0042586 | molecular_function | peptide deformylase activity |
| C | 0043686 | biological_process | co-translational protein modification |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0006412 | biological_process | translation |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0042586 | molecular_function | peptide deformylase activity |
| D | 0043686 | biological_process | co-translational protein modification |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0006412 | biological_process | translation |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0042586 | molecular_function | peptide deformylase activity |
| E | 0043686 | biological_process | co-translational protein modification |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0006412 | biological_process | translation |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0042586 | molecular_function | peptide deformylase activity |
| F | 0043686 | biological_process | co-translational protein modification |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0006412 | biological_process | translation |
| G | 0016787 | molecular_function | hydrolase activity |
| G | 0042586 | molecular_function | peptide deformylase activity |
| G | 0043686 | biological_process | co-translational protein modification |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0006412 | biological_process | translation |
| H | 0016787 | molecular_function | hydrolase activity |
| H | 0042586 | molecular_function | peptide deformylase activity |
| H | 0043686 | biological_process | co-translational protein modification |
| H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 716 |
| Chain | Residue |
| A | GLN53 |
| A | CYS101 |
| A | HIS143 |
| A | HIS147 |
| A | BB2513 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 717 |
| Chain | Residue |
| B | BB2514 |
| B | GLN53 |
| B | CYS101 |
| B | HIS143 |
| B | HIS147 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 718 |
| Chain | Residue |
| C | GLN53 |
| C | CYS101 |
| C | HIS143 |
| C | HIS147 |
| C | BB2515 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 719 |
| Chain | Residue |
| D | GLN53 |
| D | CYS101 |
| D | HIS143 |
| D | HIS147 |
| D | BB2516 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN E 720 |
| Chain | Residue |
| E | GLN53 |
| E | CYS101 |
| E | HIS143 |
| E | HIS147 |
| E | BB2517 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN F 721 |
| Chain | Residue |
| F | GLN53 |
| F | CYS101 |
| F | HIS143 |
| F | HIS147 |
| F | BB2518 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN G 722 |
| Chain | Residue |
| G | GLN53 |
| G | CYS101 |
| G | HIS143 |
| G | HIS147 |
| G | BB2519 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN H 723 |
| Chain | Residue |
| H | GLN53 |
| H | CYS101 |
| H | HIS143 |
| H | HIS147 |
| H | BB2520 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BB2 A 513 |
| Chain | Residue |
| A | GLY46 |
| A | VAL47 |
| A | GLY48 |
| A | GLN53 |
| A | TRP98 |
| A | GLY100 |
| A | CYS101 |
| A | LEU102 |
| A | TYR136 |
| A | ILE139 |
| A | VAL140 |
| A | HIS143 |
| A | GLU144 |
| A | HIS147 |
| A | ZN716 |
| site_id | BC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE BB2 B 514 |
| Chain | Residue |
| B | GLY46 |
| B | VAL47 |
| B | GLY48 |
| B | GLN53 |
| B | TYR71 |
| B | PHE97 |
| B | TRP98 |
| B | GLY100 |
| B | CYS101 |
| B | LEU102 |
| B | TYR136 |
| B | ILE139 |
| B | VAL140 |
| B | HIS143 |
| B | GLU144 |
| B | HIS147 |
| B | ZN717 |
| site_id | BC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE BB2 C 515 |
| Chain | Residue |
| C | GLY46 |
| C | VAL47 |
| C | GLY48 |
| C | GLN53 |
| C | TYR71 |
| C | TRP98 |
| C | GLU99 |
| C | GLY100 |
| C | CYS101 |
| C | LEU102 |
| C | TYR136 |
| C | ILE139 |
| C | HIS143 |
| C | GLU144 |
| C | HIS147 |
| C | ZN718 |
| site_id | BC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE BB2 D 516 |
| Chain | Residue |
| D | TYR136 |
| D | VAL140 |
| D | HIS143 |
| D | GLU144 |
| D | HIS147 |
| D | ZN719 |
| D | GLY46 |
| D | VAL47 |
| D | GLY48 |
| D | GLN53 |
| D | GLU69 |
| D | THR74 |
| D | TRP98 |
| D | GLU99 |
| D | GLY100 |
| D | CYS101 |
| D | LEU102 |
| site_id | BC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE BB2 E 517 |
| Chain | Residue |
| E | GLY46 |
| E | VAL47 |
| E | GLY48 |
| E | GLN53 |
| E | TRP98 |
| E | GLU99 |
| E | GLY100 |
| E | CYS101 |
| E | LEU102 |
| E | ILE139 |
| E | HIS143 |
| E | GLU144 |
| E | HIS147 |
| E | ZN720 |
| site_id | BC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE BB2 F 518 |
| Chain | Residue |
| F | GLY46 |
| F | VAL47 |
| F | GLY48 |
| F | GLN53 |
| F | TRP98 |
| F | GLY100 |
| F | CYS101 |
| F | LEU102 |
| F | TYR136 |
| F | HIS143 |
| F | GLU144 |
| F | HIS147 |
| F | ZN721 |
| site_id | BC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BB2 G 519 |
| Chain | Residue |
| G | VAL47 |
| G | GLY48 |
| G | GLN53 |
| G | PHE97 |
| G | TRP98 |
| G | GLU99 |
| G | GLY100 |
| G | CYS101 |
| G | LEU102 |
| G | ILE139 |
| G | VAL140 |
| G | HIS143 |
| G | GLU144 |
| G | HIS147 |
| G | ZN722 |
| site_id | BC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BB2 H 520 |
| Chain | Residue |
| H | GLY46 |
| H | VAL47 |
| H | GLY48 |
| H | GLN53 |
| H | TRP98 |
| H | GLY100 |
| H | CYS101 |
| H | LEU102 |
| H | ARG108 |
| H | TYR136 |
| H | VAL140 |
| H | HIS143 |
| H | GLU144 |
| H | HIS147 |
| H | ZN723 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU144 | |
| B | GLU144 | |
| C | GLU144 | |
| D | GLU144 | |
| E | GLU144 | |
| F | GLU144 | |
| G | GLU144 | |
| H | GLU144 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS101 | |
| D | CYS101 | |
| D | HIS143 | |
| D | HIS147 | |
| E | CYS101 | |
| E | HIS143 | |
| E | HIS147 | |
| F | CYS101 | |
| F | HIS143 | |
| F | HIS147 | |
| G | CYS101 | |
| A | HIS143 | |
| G | HIS143 | |
| G | HIS147 | |
| H | CYS101 | |
| H | HIS143 | |
| H | HIS147 | |
| A | HIS147 | |
| B | CYS101 | |
| B | HIS143 | |
| B | HIS147 | |
| C | CYS101 | |
| C | HIS143 | |
| C | HIS147 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bs4 |
| Chain | Residue | Details |
| A | LEU102 | |
| A | GLY48 | |
| A | GLN53 | |
| A | GLU144 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bs4 |
| Chain | Residue | Details |
| B | LEU102 | |
| B | GLY48 | |
| B | GLN53 | |
| B | GLU144 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bs4 |
| Chain | Residue | Details |
| C | LEU102 | |
| C | GLY48 | |
| C | GLN53 | |
| C | GLU144 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bs4 |
| Chain | Residue | Details |
| D | LEU102 | |
| D | GLY48 | |
| D | GLN53 | |
| D | GLU144 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bs4 |
| Chain | Residue | Details |
| E | LEU102 | |
| E | GLY48 | |
| E | GLN53 | |
| E | GLU144 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bs4 |
| Chain | Residue | Details |
| F | LEU102 | |
| F | GLY48 | |
| F | GLN53 | |
| F | GLU144 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bs4 |
| Chain | Residue | Details |
| G | LEU102 | |
| G | GLY48 | |
| G | GLN53 | |
| G | GLU144 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bs4 |
| Chain | Residue | Details |
| H | LEU102 | |
| H | GLY48 | |
| H | GLN53 | |
| H | GLU144 |
