3W1J
Crystal structure of the N-terminal truncated selenocysteine synthase SelA in complex with thiosulfate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001514 | biological_process | selenocysteine incorporation |
A | 0004125 | molecular_function | L-seryl-tRNA(Sec) selenium transferase activity |
A | 0005737 | cellular_component | cytoplasm |
B | 0001514 | biological_process | selenocysteine incorporation |
B | 0004125 | molecular_function | L-seryl-tRNA(Sec) selenium transferase activity |
B | 0005737 | cellular_component | cytoplasm |
C | 0001514 | biological_process | selenocysteine incorporation |
C | 0004125 | molecular_function | L-seryl-tRNA(Sec) selenium transferase activity |
C | 0005737 | cellular_component | cytoplasm |
D | 0001514 | biological_process | selenocysteine incorporation |
D | 0004125 | molecular_function | L-seryl-tRNA(Sec) selenium transferase activity |
D | 0005737 | cellular_component | cytoplasm |
E | 0001514 | biological_process | selenocysteine incorporation |
E | 0004125 | molecular_function | L-seryl-tRNA(Sec) selenium transferase activity |
E | 0005737 | cellular_component | cytoplasm |
F | 0001514 | biological_process | selenocysteine incorporation |
F | 0004125 | molecular_function | L-seryl-tRNA(Sec) selenium transferase activity |
F | 0005737 | cellular_component | cytoplasm |
G | 0001514 | biological_process | selenocysteine incorporation |
G | 0004125 | molecular_function | L-seryl-tRNA(Sec) selenium transferase activity |
G | 0005737 | cellular_component | cytoplasm |
H | 0001514 | biological_process | selenocysteine incorporation |
H | 0004125 | molecular_function | L-seryl-tRNA(Sec) selenium transferase activity |
H | 0005737 | cellular_component | cytoplasm |
I | 0001514 | biological_process | selenocysteine incorporation |
I | 0004125 | molecular_function | L-seryl-tRNA(Sec) selenium transferase activity |
I | 0005737 | cellular_component | cytoplasm |
J | 0001514 | biological_process | selenocysteine incorporation |
J | 0004125 | molecular_function | L-seryl-tRNA(Sec) selenium transferase activity |
J | 0005737 | cellular_component | cytoplasm |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K A 2001 |
Chain | Residue |
A | ASN140 |
A | ASP317 |
B | ASN140 |
B | ASP317 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE THJ A 2002 |
Chain | Residue |
B | ARG312 |
B | ARG315 |
A | THR82 |
A | ARG86 |
A | ILE169 |
A | GLY170 |
B | GLU108 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE THJ A 2003 |
Chain | Residue |
A | THR76 |
A | ASN81 |
A | ASN83 |
B | TYR109 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE THJ A 2004 |
Chain | Residue |
A | ILE80 |
A | ASN81 |
A | THR82 |
A | GLY382 |
A | GLY383 |
J | PHE224 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE THJ B 501 |
Chain | Residue |
A | TYR109 |
B | THR76 |
B | ASN81 |
B | ASN83 |
B | VAL419 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE THJ C 501 |
Chain | Residue |
C | THR82 |
C | GLY170 |
D | GLU108 |
D | ARG312 |
D | ARG315 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE K D 501 |
Chain | Residue |
C | ASN140 |
D | ASN140 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE THJ D 502 |
Chain | Residue |
C | GLU108 |
C | ARG312 |
C | ARG315 |
D | THR82 |
D | ILE169 |
D | GLY170 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE THJ D 503 |
Chain | Residue |
C | TYR109 |
D | ASN81 |
D | ASN83 |
D | LEU84 |
D | VAL419 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K E 501 |
Chain | Residue |
E | ASN140 |
E | ASP317 |
F | ASN140 |
F | ASP317 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE THJ E 502 |
Chain | Residue |
E | THR82 |
E | ARG86 |
E | ILE169 |
E | GLY170 |
F | GLU108 |
F | ARG312 |
F | ARG315 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE THJ E 503 |
Chain | Residue |
E | ASN81 |
E | ASN83 |
E | LEU84 |
E | THJ504 |
F | TYR109 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE THJ E 504 |
Chain | Residue |
D | PHE224 |
E | ASN81 |
E | THR82 |
E | GLY382 |
E | THJ503 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K G 501 |
Chain | Residue |
G | ASN140 |
G | ASP317 |
H | ASN140 |
H | ASP317 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE THJ H 501 |
Chain | Residue |
G | TYR109 |
H | THR76 |
H | ASN81 |
H | ASN83 |
H | LEU84 |
H | VAL419 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K I 501 |
Chain | Residue |
I | ASN140 |
I | ASP317 |
J | ASN140 |
J | ASP317 |
site_id | BC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE THJ I 502 |
Chain | Residue |
I | THR82 |
I | ARG86 |
I | ILE169 |
I | GLY170 |
J | GLU108 |
J | ARG312 |
J | ARG315 |
site_id | BC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE THJ I 503 |
Chain | Residue |
I | ASN81 |
I | ASN83 |
J | TYR109 |
site_id | CC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE THJ J 501 |
Chain | Residue |
I | GLU108 |
I | ARG312 |
I | ARG315 |
J | THR82 |
J | ARG86 |
J | ILE169 |
J | GLY170 |
J | GLY171 |
site_id | CC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE THJ J 502 |
Chain | Residue |
J | ASN81 |
J | ASN83 |
J | LEU84 |
J | THJ503 |
I | TYR109 |
J | THR76 |
site_id | CC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE THJ J 503 |
Chain | Residue |
A | PHE224 |
J | VAL78 |
J | ILE80 |
J | ASN81 |
J | THR82 |
J | GLY382 |
J | THJ502 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00423 |
Chain | Residue | Details |
A | LLP285 | |
J | LLP285 | |
B | LLP285 | |
C | LLP285 | |
D | LLP285 | |
E | LLP285 | |
F | LLP285 | |
G | LLP285 | |
H | LLP285 | |
I | LLP285 |