1QJG
Crystal structure of delta5-3-ketosteroid isomerase from Pseudomonas testosteroni in complex with 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 1140 |
Chain | Residue |
B | HIS6 |
B | ARG13 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EQU A 130 |
Chain | Residue |
A | TYR14 |
A | ASN38 |
A | PHE82 |
A | PHE86 |
A | ASP99 |
A | MET112 |
A | PHE116 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE EQU B 130 |
Chain | Residue |
B | TYR14 |
B | ASN38 |
B | SER58 |
B | PHE82 |
B | VAL84 |
B | VAL95 |
B | ASP99 |
B | MET112 |
B | PHE116 |
B | HOH2044 |
D | ARG13 |
D | ALA20 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EQU C 130 |
Chain | Residue |
C | TYR14 |
C | ASN38 |
C | PHE82 |
C | PRO97 |
C | ASP99 |
C | MET112 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EQU D 130 |
Chain | Residue |
D | TYR14 |
D | ASN38 |
D | PHE86 |
D | ASP99 |
D | MET112 |
D | PHE116 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EQU E 130 |
Chain | Residue |
C | ALA20 |
C | HOH2006 |
E | TYR14 |
E | ASN38 |
E | LEU61 |
E | ASP99 |
E | MET112 |
E | PHE116 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EQU F 130 |
Chain | Residue |
F | TYR14 |
F | ASN38 |
F | PHE86 |
F | ASP99 |
F | MET112 |
F | PHE116 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | TYR14 | |
B | TYR14 | |
C | TYR14 | |
D | TYR14 | |
E | TYR14 | |
F | TYR14 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:3480517 |
Chain | Residue | Details |
A | ASN38 | |
B | ASN38 | |
C | ASN38 | |
D | ASN38 | |
E | ASN38 | |
F | ASN38 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP99 | |
B | ASP99 | |
C | ASP99 | |
D | ASP99 | |
E | ASP99 | |
F | ASP99 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1e3v |
Chain | Residue | Details |
A | ASN38 | |
A | PHE30 | |
A | TYR14 | |
A | ASP99 | |
A | TYR55 |
site_id | CSA2 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1e3v |
Chain | Residue | Details |
B | ASN38 | |
B | PHE30 | |
B | TYR14 | |
B | ASP99 | |
B | TYR55 |
site_id | CSA3 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1e3v |
Chain | Residue | Details |
C | ASN38 | |
C | PHE30 | |
C | TYR14 | |
C | ASP99 | |
C | TYR55 |
site_id | CSA4 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1e3v |
Chain | Residue | Details |
D | ASN38 | |
D | PHE30 | |
D | TYR14 | |
D | ASP99 | |
D | TYR55 |
site_id | CSA5 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1e3v |
Chain | Residue | Details |
E | ASN38 | |
E | PHE30 | |
E | TYR14 | |
E | ASP99 | |
E | TYR55 |
site_id | CSA6 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1e3v |
Chain | Residue | Details |
F | ASN38 | |
F | PHE30 | |
F | TYR14 | |
F | ASP99 | |
F | TYR55 |