2ZP7
Crystal structure of LysN, alpha-aminoadipate aminotransferase (Leucine complex), from Thermus thermophilus HB27
Replaces: 2ZG5Replaces: 2DTVFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| 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 |
| A | 1901605 | biological_process | alpha-amino acid metabolic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| 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 |
| B | 1901605 | biological_process | alpha-amino acid metabolic process |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| 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 |
| C | 1901605 | biological_process | alpha-amino acid metabolic process |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| 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 |
| D | 1901605 | biological_process | alpha-amino acid metabolic process |
| E | 0008483 | molecular_function | transaminase activity |
| E | 0009058 | biological_process | biosynthetic process |
| E | 0016740 | molecular_function | transferase activity |
| E | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| E | 0030170 | molecular_function | pyridoxal phosphate binding |
| E | 0047536 | molecular_function | 2-aminoadipate transaminase activity |
| E | 1901605 | biological_process | alpha-amino acid metabolic process |
| F | 0008483 | molecular_function | transaminase activity |
| F | 0009058 | biological_process | biosynthetic process |
| F | 0016740 | molecular_function | transferase activity |
| F | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| F | 0030170 | molecular_function | pyridoxal phosphate binding |
| F | 0047536 | molecular_function | 2-aminoadipate transaminase activity |
| F | 1901605 | biological_process | alpha-amino acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP A 600 |
| Chain | Residue |
| A | GLY99 |
| A | SER237 |
| A | LYS238 |
| A | ARG245 |
| A | LEU700 |
| C | TYR70 |
| A | SER100 |
| A | GLN101 |
| A | TYR125 |
| A | ILE169 |
| A | ASN174 |
| A | ASP202 |
| A | TYR205 |
| A | SER235 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE LEU A 700 |
| Chain | Residue |
| A | GLY39 |
| A | GLY40 |
| A | ASN174 |
| A | LYS238 |
| A | ARG368 |
| C | TYR70 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP B 600 |
| Chain | Residue |
| B | GLY99 |
| B | SER100 |
| B | GLN101 |
| B | TYR125 |
| B | ILE169 |
| B | ASN174 |
| B | ASP202 |
| B | TYR205 |
| B | SER235 |
| B | SER237 |
| B | LYS238 |
| B | ARG245 |
| B | LEU700 |
| D | TYR70 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE LEU B 700 |
| Chain | Residue |
| B | GLY39 |
| B | GLY40 |
| B | ASN174 |
| B | LYS238 |
| B | ARG368 |
| D | TYR70 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP C 600 |
| Chain | Residue |
| A | TYR70 |
| C | GLY99 |
| C | SER100 |
| C | GLN101 |
| C | TYR125 |
| C | ILE169 |
| C | ASN174 |
| C | ASP202 |
| C | TYR205 |
| C | SER235 |
| C | SER237 |
| C | LYS238 |
| C | ARG245 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP D 600 |
| Chain | Residue |
| B | TYR70 |
| D | GLY99 |
| D | SER100 |
| D | GLN101 |
| D | TYR125 |
| D | ILE169 |
| D | ASN174 |
| D | ASP202 |
| D | TYR205 |
| D | SER235 |
| D | SER237 |
| D | LYS238 |
| D | ARG245 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP E 600 |
| Chain | Residue |
| E | GLY99 |
| E | SER100 |
| E | GLN101 |
| E | TYR125 |
| E | ILE169 |
| E | ASN174 |
| E | ASP202 |
| E | TYR205 |
| E | SER235 |
| E | SER237 |
| E | LYS238 |
| E | ARG245 |
| E | LEU700 |
| F | TYR70 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE LEU E 700 |
| Chain | Residue |
| E | GLY40 |
| E | TYR125 |
| E | ASN174 |
| E | LYS238 |
| E | ARG368 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP F 600 |
| Chain | Residue |
| E | TYR70 |
| E | LEU268 |
| F | GLY99 |
| F | SER100 |
| F | GLN101 |
| F | TYR125 |
| F | ASN174 |
| F | ASP202 |
| F | TYR205 |
| F | SER235 |
| F | SER237 |
| F | LYS238 |
| F | ARG245 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18831049","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19632206","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of lysN, alpha-aminoadipate aminotransferase, from Thermus thermophilus HB27.","authors":["Tomita T.","Miyazaki T.","Miyagawa T.","Fushinobu S.","Kuzuyama T.","Nishiyama M."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 36 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Site: {"description":"Recognizes the side-chain carboxyl group of acidic compounds"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
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 | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| D | TYR125 | |
| D | ASP202 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| E | TYR125 | |
| E | ASP202 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| F | TYR125 | |
| F | 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 | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| E | LYS238 | |
| E | TYR125 | |
| E | ASP202 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| F | LYS238 | |
| F | TYR125 | |
| F | ASP202 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TYR125 | |
| A | ASP202 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TYR125 | |
| B | ASP202 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | TYR125 | |
| C | ASP202 |
