1TJW
Crystal Structure of T161D Duck Delta 2 Crystallin Mutant with bound argininosuccinate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004056 | molecular_function | argininosuccinate lyase activity |
A | 0005212 | molecular_function | structural constituent of eye lens |
A | 0005829 | cellular_component | cytosol |
A | 0006526 | biological_process | arginine biosynthetic process |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0042450 | biological_process | arginine biosynthetic process via ornithine |
B | 0003824 | molecular_function | catalytic activity |
B | 0004056 | molecular_function | argininosuccinate lyase activity |
B | 0005212 | molecular_function | structural constituent of eye lens |
B | 0005829 | cellular_component | cytosol |
B | 0006526 | biological_process | arginine biosynthetic process |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0016829 | molecular_function | lyase activity |
B | 0042450 | biological_process | arginine biosynthetic process via ornithine |
C | 0003824 | molecular_function | catalytic activity |
C | 0004056 | molecular_function | argininosuccinate lyase activity |
C | 0005212 | molecular_function | structural constituent of eye lens |
C | 0005829 | cellular_component | cytosol |
C | 0006526 | biological_process | arginine biosynthetic process |
C | 0008652 | biological_process | amino acid biosynthetic process |
C | 0016829 | molecular_function | lyase activity |
C | 0042450 | biological_process | arginine biosynthetic process via ornithine |
D | 0003824 | molecular_function | catalytic activity |
D | 0004056 | molecular_function | argininosuccinate lyase activity |
D | 0005212 | molecular_function | structural constituent of eye lens |
D | 0005829 | cellular_component | cytosol |
D | 0006526 | biological_process | arginine biosynthetic process |
D | 0008652 | biological_process | amino acid biosynthetic process |
D | 0016829 | molecular_function | lyase activity |
D | 0042450 | biological_process | arginine biosynthetic process via ornithine |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE AS1 C 1001 |
Chain | Residue |
A | HIS162 |
C | LYS331 |
C | HOH1064 |
C | HOH1068 |
C | HOH1078 |
C | HOH1167 |
C | HOH1236 |
C | HOH1256 |
A | HOH1078 |
C | SER29 |
C | SER114 |
C | ARG115 |
C | ASN116 |
C | ALA205 |
C | TYR323 |
C | GLN328 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE AS1 D 1002 |
Chain | Residue |
B | HIS162 |
B | HOH1064 |
D | SER29 |
D | SER114 |
D | ARG115 |
D | ASN116 |
D | ALA205 |
D | TYR323 |
D | GLN328 |
D | LYS331 |
D | HOH1044 |
D | HOH1083 |
D | HOH1097 |
D | HOH1132 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE AS1 B 1003 |
Chain | Residue |
B | SER29 |
B | SER114 |
B | ARG115 |
B | ASN116 |
B | ALA205 |
B | TYR323 |
B | GLN328 |
B | LYS331 |
B | HOH1046 |
B | HOH1053 |
B | HOH1054 |
B | HOH1068 |
B | HOH1131 |
B | HOH1147 |
D | HIS162 |
site_id | AC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE AS1 A 1004 |
Chain | Residue |
A | SER29 |
A | SER114 |
A | ARG115 |
A | ASN116 |
A | ALA205 |
A | TYR323 |
A | GLN328 |
A | LYS331 |
A | HOH1036 |
A | HOH1066 |
A | HOH1073 |
A | HOH1114 |
A | HOH1203 |
A | HOH1215 |
A | HOH1243 |
C | HIS162 |
C | HOH1106 |
C | HOH1164 |
Functional Information from PROSITE/UniProt
site_id | PS00163 |
Number of Residues | 10 |
Details | FUMARATE_LYASES Fumarate lyases signature. GSslMpQKkN |
Chain | Residue | Details |
A | GLY282-ASN291 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:11698398 |
Chain | Residue | Details |
A | HIS162 | |
B | HIS162 | |
C | HIS162 | |
D | HIS162 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:11698398 |
Chain | Residue | Details |
A | SER283 | |
B | SER283 | |
C | SER283 | |
D | SER283 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: in chain A => ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1K7W |
Chain | Residue | Details |
C | SER29 | |
C | ASN116 | |
D | SER29 | |
D | ASN116 | |
A | SER29 | |
A | ASN116 | |
B | SER29 | |
B | ASN116 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: in chain C => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W |
Chain | Residue | Details |
A | ASP161 | |
B | ASP161 | |
C | ASP161 | |
D | ASP161 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: in chain B => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W |
Chain | Residue | Details |
A | ASN291 | |
B | ASN291 | |
C | ASN291 | |
D | ASN291 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | BINDING: in chain A => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W |
Chain | Residue | Details |
C | TYR323 | |
C | LYS331 | |
D | TYR323 | |
D | LYS331 | |
A | TYR323 | |
A | LYS331 | |
B | TYR323 | |
B | LYS331 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | BINDING: in chain A => ECO:0000269|PubMed:10029536, ECO:0007744|PDB:1DCN |
Chain | Residue | Details |
A | GLN328 | |
B | GLN328 | |
C | GLN328 | |
D | GLN328 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | SITE: Increases basicity of active site His => ECO:0000305|PubMed:11698398 |
Chain | Residue | Details |
A | GLU296 | |
B | GLU296 | |
C | GLU296 | |
D | GLU296 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 408 |
Chain | Residue | Details |
A | HIS162 | proton shuttle (general acid/base) |
A | SER283 | proton shuttle (general acid/base) |
A | LYS289 | electrostatic stabiliser |
A | GLU296 | activator, proton shuttle (general acid/base) |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 408 |
Chain | Residue | Details |
B | HIS162 | proton shuttle (general acid/base) |
B | SER283 | proton shuttle (general acid/base) |
B | LYS289 | electrostatic stabiliser |
B | GLU296 | activator, proton shuttle (general acid/base) |
site_id | MCSA3 |
Number of Residues | 4 |
Details | M-CSA 408 |
Chain | Residue | Details |
C | HIS162 | proton shuttle (general acid/base) |
C | SER283 | proton shuttle (general acid/base) |
C | LYS289 | electrostatic stabiliser |
C | GLU296 | activator, proton shuttle (general acid/base) |
site_id | MCSA4 |
Number of Residues | 4 |
Details | M-CSA 408 |
Chain | Residue | Details |
D | HIS162 | proton shuttle (general acid/base) |
D | SER283 | proton shuttle (general acid/base) |
D | LYS289 | electrostatic stabiliser |
D | GLU296 | activator, proton shuttle (general acid/base) |