2EGY
Crystal structure of LysN, alpha-aminoadipate aminotransferase (substrate free form), from Thermus thermophilus HB27
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008483 | molecular_function | transaminase activity |
A | 0009058 | biological_process | biosynthetic process |
A | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0047536 | molecular_function | 2-aminoadipate transaminase activity |
B | 0008483 | molecular_function | transaminase activity |
B | 0009058 | biological_process | biosynthetic process |
B | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0047536 | molecular_function | 2-aminoadipate transaminase activity |
C | 0008483 | molecular_function | transaminase activity |
C | 0009058 | biological_process | biosynthetic process |
C | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
C | 0030170 | molecular_function | pyridoxal phosphate binding |
C | 0047536 | molecular_function | 2-aminoadipate transaminase activity |
D | 0008483 | molecular_function | transaminase activity |
D | 0009058 | biological_process | biosynthetic process |
D | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
D | 0030170 | molecular_function | pyridoxal phosphate binding |
D | 0047536 | molecular_function | 2-aminoadipate transaminase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PLP A 400 |
Chain | Residue |
A | GLY99 |
A | SER237 |
A | LYS238 |
A | ARG245 |
B | TYR70 |
A | SER100 |
A | GLN101 |
A | TYR125 |
A | ASN174 |
A | ASP202 |
A | ALA204 |
A | TYR205 |
A | SER235 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PLP B 400 |
Chain | Residue |
A | TYR70 |
B | GLY99 |
B | SER100 |
B | GLN101 |
B | TYR125 |
B | ASN174 |
B | ASP202 |
B | ALA204 |
B | TYR205 |
B | SER235 |
B | SER237 |
B | LYS238 |
B | ARG245 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PLP C 400 |
Chain | Residue |
C | GLY99 |
C | SER100 |
C | GLN101 |
C | TYR125 |
C | ILE169 |
C | ASN174 |
C | ASP202 |
C | ALA204 |
C | TYR205 |
C | SER235 |
C | SER237 |
C | LYS238 |
C | ARG245 |
D | TYR70 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PLP D 400 |
Chain | Residue |
C | TYR70 |
D | GLY99 |
D | SER100 |
D | GLN101 |
D | ASN174 |
D | ASP202 |
D | ALA204 |
D | TYR205 |
D | SER235 |
D | SER237 |
D | LYS238 |
D | ARG245 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18831049, ECO:0000269|PubMed:19632206 |
Chain | Residue | Details |
A | GLY40 | |
D | GLY40 | |
D | ASN174 | |
D | ARG368 | |
A | ASN174 | |
A | ARG368 | |
B | GLY40 | |
B | ASN174 | |
B | ARG368 | |
C | GLY40 | |
C | ASN174 | |
C | ARG368 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|Ref.5 |
Chain | Residue | Details |
A | TYR70 | |
A | ARG245 | |
B | TYR70 | |
B | ARG245 | |
C | TYR70 | |
C | ARG245 | |
D | TYR70 | |
D | ARG245 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: |
Chain | Residue | Details |
A | SER100 | |
D | SER100 | |
D | ASP202 | |
D | SER235 | |
A | ASP202 | |
A | SER235 | |
B | SER100 | |
B | ASP202 | |
B | SER235 | |
C | SER100 | |
C | ASP202 | |
C | SER235 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Recognizes the side-chain carboxyl group of acidic compounds |
Chain | Residue | Details |
A | ARG23 | |
B | ARG23 | |
C | ARG23 | |
D | ARG23 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
Chain | Residue | Details |
A | LYS263 | |
B | LYS263 | |
C | LYS263 | |
D | LYS263 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | LYS238 | |
A | TYR125 | |
A | ASP202 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
B | LYS238 | |
B | TYR125 | |
B | ASP202 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
C | LYS238 | |
C | TYR125 | |
C | ASP202 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
D | LYS238 | |
D | TYR125 | |
D | ASP202 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | TYR125 | |
A | ASP202 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
B | TYR125 | |
B | ASP202 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
C | TYR125 | |
C | ASP202 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
D | TYR125 | |
D | ASP202 |