1K1D
Crystal structure of D-hydantoinase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
A | 0046872 | molecular_function | metal ion binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
B | 0046872 | molecular_function | metal ion binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
C | 0046872 | molecular_function | metal ion binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0016787 | molecular_function | hydrolase activity |
D | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
D | 0046872 | molecular_function | metal ion binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0016787 | molecular_function | hydrolase activity |
E | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
E | 0046872 | molecular_function | metal ion binding |
F | 0005737 | cellular_component | cytoplasm |
F | 0016787 | molecular_function | hydrolase activity |
F | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
F | 0046872 | molecular_function | metal ion binding |
G | 0005737 | cellular_component | cytoplasm |
G | 0016787 | molecular_function | hydrolase activity |
G | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
G | 0046872 | molecular_function | metal ion binding |
H | 0005737 | cellular_component | cytoplasm |
H | 0016787 | molecular_function | hydrolase activity |
H | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 501 |
Chain | Residue |
A | KCX150 |
A | HIS183 |
A | HIS239 |
A | ZN502 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 502 |
Chain | Residue |
A | HIS58 |
A | HIS60 |
A | KCX150 |
A | ASP315 |
A | ZN501 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 501 |
Chain | Residue |
B | KCX150 |
B | HIS183 |
B | HIS239 |
B | ZN502 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 502 |
Chain | Residue |
B | HIS58 |
B | HIS60 |
B | KCX150 |
B | ASP315 |
B | ZN501 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 501 |
Chain | Residue |
C | KCX150 |
C | HIS183 |
C | HIS239 |
C | ZN502 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 502 |
Chain | Residue |
C | HIS58 |
C | HIS60 |
C | KCX150 |
C | ASP315 |
C | ZN501 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 501 |
Chain | Residue |
D | KCX150 |
D | HIS183 |
D | HIS239 |
D | ZN502 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN D 502 |
Chain | Residue |
D | HIS58 |
D | HIS60 |
D | KCX150 |
D | ASP315 |
D | ZN501 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN E 501 |
Chain | Residue |
E | KCX150 |
E | HIS183 |
E | HIS239 |
E | ZN502 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN E 502 |
Chain | Residue |
E | HIS58 |
E | HIS60 |
E | KCX150 |
E | ASP315 |
E | ZN501 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN F 501 |
Chain | Residue |
F | KCX150 |
F | HIS183 |
F | HIS239 |
F | ZN502 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN F 502 |
Chain | Residue |
F | HIS58 |
F | HIS60 |
F | KCX150 |
F | ASP315 |
F | ZN501 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN G 501 |
Chain | Residue |
G | KCX150 |
G | HIS183 |
G | HIS239 |
G | ZN502 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN G 502 |
Chain | Residue |
G | HIS58 |
G | HIS60 |
G | KCX150 |
G | ASP315 |
G | ZN501 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN H 501 |
Chain | Residue |
H | KCX150 |
H | HIS183 |
H | HIS239 |
H | ZN502 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN H 502 |
Chain | Residue |
H | HIS58 |
H | HIS60 |
H | KCX150 |
H | ASP315 |
H | ZN501 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 40 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12135362, ECO:0007744|PDB:1K1D |
Chain | Residue | Details |
A | HIS58 | |
B | ASP315 | |
C | HIS58 | |
C | HIS60 | |
C | HIS183 | |
C | HIS239 | |
C | ASP315 | |
D | HIS58 | |
D | HIS60 | |
D | HIS183 | |
D | HIS239 | |
A | HIS60 | |
D | ASP315 | |
E | HIS58 | |
E | HIS60 | |
E | HIS183 | |
E | HIS239 | |
E | ASP315 | |
F | HIS58 | |
F | HIS60 | |
F | HIS183 | |
F | HIS239 | |
A | HIS183 | |
F | ASP315 | |
G | HIS58 | |
G | HIS60 | |
G | HIS183 | |
G | HIS239 | |
G | ASP315 | |
H | HIS58 | |
H | HIS60 | |
H | HIS183 | |
H | HIS239 | |
A | HIS239 | |
H | ASP315 | |
A | ASP315 | |
B | HIS58 | |
B | HIS60 | |
B | HIS183 | |
B | HIS239 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: via carbamate group => ECO:0000269|PubMed:12135362, ECO:0007744|PDB:1K1D |
Chain | Residue | Details |
A | KCX150 | |
B | KCX150 | |
C | KCX150 | |
D | KCX150 | |
E | KCX150 | |
F | KCX150 | |
G | KCX150 | |
H | KCX150 |
site_id | SWS_FT_FI3 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9P903 |
Chain | Residue | Details |
A | TYR155 | |
D | TYR155 | |
D | SER288 | |
D | ASN337 | |
E | TYR155 | |
E | SER288 | |
E | ASN337 | |
F | TYR155 | |
F | SER288 | |
F | ASN337 | |
G | TYR155 | |
A | SER288 | |
G | SER288 | |
G | ASN337 | |
H | TYR155 | |
H | SER288 | |
H | ASN337 | |
A | ASN337 | |
B | TYR155 | |
B | SER288 | |
B | ASN337 | |
C | TYR155 | |
C | SER288 | |
C | ASN337 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:12135362 |
Chain | Residue | Details |
A | KCX150 | |
B | KCX150 | |
C | KCX150 | |
D | KCX150 | |
E | KCX150 | |
F | KCX150 | |
G | KCX150 | |
H | KCX150 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1j79 |
Chain | Residue | Details |
A | ASP315 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1j79 |
Chain | Residue | Details |
B | ASP315 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1j79 |
Chain | Residue | Details |
C | ASP315 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1j79 |
Chain | Residue | Details |
D | ASP315 |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1j79 |
Chain | Residue | Details |
E | ASP315 |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1j79 |
Chain | Residue | Details |
F | ASP315 |
site_id | CSA7 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1j79 |
Chain | Residue | Details |
G | ASP315 |
site_id | CSA8 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1j79 |
Chain | Residue | Details |
H | ASP315 |