3OWY
Crystal Structure of Ketosteroid Isomerase D40N/C69S/C81S/C97S/M105C-CN from P. putida with Bound Equilenin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004769 | molecular_function | steroid delta-isomerase activity |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0016853 | molecular_function | isomerase activity |
| B | 0004769 | molecular_function | steroid delta-isomerase activity |
| B | 0008202 | biological_process | steroid metabolic process |
| B | 0016853 | molecular_function | isomerase activity |
| C | 0004769 | molecular_function | steroid delta-isomerase activity |
| C | 0008202 | biological_process | steroid metabolic process |
| C | 0016853 | molecular_function | isomerase activity |
| D | 0004769 | molecular_function | steroid delta-isomerase activity |
| D | 0008202 | biological_process | steroid metabolic process |
| D | 0016853 | molecular_function | isomerase activity |
| E | 0004769 | molecular_function | steroid delta-isomerase activity |
| E | 0008202 | biological_process | steroid metabolic process |
| E | 0016853 | molecular_function | isomerase activity |
| F | 0004769 | molecular_function | steroid delta-isomerase activity |
| F | 0008202 | biological_process | steroid metabolic process |
| F | 0016853 | molecular_function | isomerase activity |
| G | 0004769 | molecular_function | steroid delta-isomerase activity |
| G | 0008202 | biological_process | steroid metabolic process |
| G | 0016853 | molecular_function | isomerase activity |
| H | 0004769 | molecular_function | steroid delta-isomerase activity |
| H | 0008202 | biological_process | steroid metabolic process |
| H | 0016853 | molecular_function | isomerase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EQU A 200 |
| Chain | Residue |
| A | TYR16 |
| A | ASN40 |
| A | MET90 |
| A | LEU99 |
| A | ASP103 |
| A | TRP120 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EQU B 200 |
| Chain | Residue |
| B | PHE86 |
| B | LEU99 |
| B | ASP103 |
| B | TRP120 |
| B | TYR16 |
| B | ASN40 |
| B | GLY60 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EQU C 200 |
| Chain | Residue |
| C | TYR16 |
| C | ASN40 |
| C | LEU99 |
| C | ASP103 |
| C | MET116 |
| C | TRP120 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EQU D 200 |
| Chain | Residue |
| D | TYR16 |
| D | ASN40 |
| D | GLY60 |
| D | PHE86 |
| D | ASP103 |
| D | MET116 |
| D | TRP120 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EQU E 200 |
| Chain | Residue |
| E | TYR16 |
| E | ASN40 |
| E | PHE86 |
| E | LEU99 |
| E | ASP103 |
| E | MET116 |
| E | TRP120 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EQU H 200 |
| Chain | Residue |
| H | TYR16 |
| H | ASN40 |
| H | PHE86 |
| H | ASP103 |
| H | TRP120 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | TYR16 | |
| B | TYR16 | |
| C | TYR16 | |
| D | TYR16 | |
| E | TYR16 | |
| F | TYR16 | |
| G | TYR16 | |
| H | TYR16 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | ASN40 | |
| B | ASN40 | |
| C | ASN40 | |
| D | ASN40 | |
| E | ASN40 | |
| F | ASN40 | |
| G | ASN40 | |
| H | ASN40 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11007792 |
| Chain | Residue | Details |
| A | ASP103 | |
| B | ASP103 | |
| C | ASP103 | |
| D | ASP103 | |
| E | ASP103 | |
| F | ASP103 | |
| G | ASP103 | |
| H | ASP103 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 349 |
| Chain | Residue | Details |
| A | TYR16 | proton acceptor, proton donor |
| A | ASN40 | proton acceptor, proton donor |
| A | ASP100 | electrostatic stabiliser |
| A | ASP103 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 349 |
| Chain | Residue | Details |
| B | TYR16 | proton acceptor, proton donor |
| B | ASN40 | proton acceptor, proton donor |
| B | ASP100 | electrostatic stabiliser |
| B | ASP103 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 349 |
| Chain | Residue | Details |
| C | TYR16 | proton acceptor, proton donor |
| C | ASN40 | proton acceptor, proton donor |
| C | ASP100 | electrostatic stabiliser |
| C | ASP103 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 349 |
| Chain | Residue | Details |
| D | TYR16 | proton acceptor, proton donor |
| D | ASN40 | proton acceptor, proton donor |
| D | ASP100 | electrostatic stabiliser |
| D | ASP103 | electrostatic stabiliser |
| site_id | MCSA5 |
| Number of Residues | 4 |
| Details | M-CSA 349 |
| Chain | Residue | Details |
| E | TYR16 | proton acceptor, proton donor |
| E | ASN40 | proton acceptor, proton donor |
| E | ASP100 | electrostatic stabiliser |
| E | ASP103 | electrostatic stabiliser |
| site_id | MCSA6 |
| Number of Residues | 4 |
| Details | M-CSA 349 |
| Chain | Residue | Details |
| F | TYR16 | proton acceptor, proton donor |
| F | ASN40 | proton acceptor, proton donor |
| F | ASP100 | electrostatic stabiliser |
| F | ASP103 | electrostatic stabiliser |
| site_id | MCSA7 |
| Number of Residues | 4 |
| Details | M-CSA 349 |
| Chain | Residue | Details |
| G | TYR16 | proton acceptor, proton donor |
| G | ASN40 | proton acceptor, proton donor |
| G | ASP100 | electrostatic stabiliser |
| G | ASP103 | electrostatic stabiliser |
| site_id | MCSA8 |
| Number of Residues | 4 |
| Details | M-CSA 349 |
| Chain | Residue | Details |
| H | TYR16 | proton acceptor, proton donor |
| H | ASN40 | proton acceptor, proton donor |
| H | ASP100 | electrostatic stabiliser |
| H | ASP103 | electrostatic stabiliser |
