2ZAD
Crystal Structure of Muconate Cycloisomerase from Thermotoga maritima MSB8
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016854 | molecular_function | racemase and epimerase activity |
| A | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| A | 0016998 | biological_process | cell wall macromolecule catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071555 | biological_process | cell wall organization |
| A | 0103031 | molecular_function | L-Ala-D/L-Glu epimerase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016854 | molecular_function | racemase and epimerase activity |
| B | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| B | 0016998 | biological_process | cell wall macromolecule catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071555 | biological_process | cell wall organization |
| B | 0103031 | molecular_function | L-Ala-D/L-Glu epimerase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0016854 | molecular_function | racemase and epimerase activity |
| C | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| C | 0016998 | biological_process | cell wall macromolecule catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0071555 | biological_process | cell wall organization |
| C | 0103031 | molecular_function | L-Ala-D/L-Glu epimerase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0016854 | molecular_function | racemase and epimerase activity |
| D | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| D | 0016998 | biological_process | cell wall macromolecule catabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0071555 | biological_process | cell wall organization |
| D | 0103031 | molecular_function | L-Ala-D/L-Glu epimerase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 346 |
| Chain | Residue |
| B | ASP188 |
| B | GLU216 |
| B | ASP241 |
| B | HOH765 |
| B | HOH766 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 346 |
| Chain | Residue |
| A | HOH642 |
| A | ASP188 |
| A | GLU216 |
| A | ASP241 |
| A | HOH523 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN C 346 |
| Chain | Residue |
| C | ASP188 |
| C | GLU216 |
| C | ASP241 |
| C | HOH668 |
| C | HOH669 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN D 346 |
| Chain | Residue |
| D | ASP188 |
| D | GLU216 |
| D | ASP241 |
| D | HOH795 |
| D | HOH907 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 1PE C 347 |
| Chain | Residue |
| C | LYS167 |
| C | ILE170 |
| C | TYR206 |
| C | GLN207 |
| C | GLY209 |
| C | ILE210 |
| C | ASP211 |
| C | HOH535 |
| C | HOH576 |
| C | HOH662 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 1PE D 347 |
| Chain | Residue |
| D | GLU130 |
| D | ARG156 |
| D | LYS184 |
| D | GLU314 |
| D | PHE315 |
| D | HOH760 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 1PE A 347 |
| Chain | Residue |
| A | ILE170 |
| A | TYR206 |
| A | GLN207 |
| A | GLY209 |
| A | ILE210 |
| A | ASP211 |
| A | HOH513 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 1PE D 348 |
| Chain | Residue |
| D | LYS228 |
| D | PHE229 |
| D | PHE232 |
| D | HIS233 |
| D | GLU257 |
| D | HOH767 |
| D | HOH851 |
| D | HOH854 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 1PE B 347 |
| Chain | Residue |
| B | LYS167 |
| B | ILE170 |
| B | TYR206 |
| B | GLN207 |
| B | GLY209 |
| B | ILE210 |
| B | ASP211 |
| B | HOH654 |
| B | HOH733 |
| B | HOH736 |
| site_id | BC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 1PE A 348 |
| Chain | Residue |
| A | GLU152 |
| A | GLU153 |
| A | PHE155 |
| A | LEU322 |
| A | GLY337 |
| A | HOH488 |
| A | HOH506 |
| A | HOH517 |
| A | HOH564 |
| D | LYS149 |
| D | GLU152 |
| D | GLU153 |
| D | PHE155 |
| D | LEU322 |
| D | GLY337 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 1PE D 349 |
| Chain | Residue |
| D | LYS167 |
| D | TYR206 |
| D | GLN207 |
| D | GLY209 |
| D | ILE210 |
| D | ASP211 |
| D | HOH742 |
| D | HOH831 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 1PE A 349 |
| Chain | Residue |
| A | GLU130 |
| A | ARG156 |
| A | LYS184 |
| A | GLU314 |
| A | PHE315 |
| A | HOH482 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 1PE B 348 |
| Chain | Residue |
| B | LEU298 |
| B | PHE329 |
| B | ARG330 |
| B | GLY331 |
| B | LYS332 |
| B | HOH633 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE 1PE C 348 |
| Chain | Residue |
| C | HOH606 |
| C | PHE329 |
| C | ARG330 |
| C | GLY331 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 1PE C 349 |
| Chain | Residue |
| C | ARG156 |
| C | LYS184 |
| C | GLU314 |
| C | PHE315 |
| C | HOH467 |
| C | HOH647 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG D 350 |
| Chain | Residue |
| D | TYR46 |
| D | LEU298 |
| D | ARG330 |
| D | HOH857 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG B 349 |
| Chain | Residue |
| A | TYR82 |
| B | TYR82 |
| B | HOH649 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 351 |
| Chain | Residue |
| A | PHE53 |
| A | ARG59 |
| B | GLU72 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor; specific for (R)-substrate epimerization => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS161 | |
| B | LYS161 | |
| C | LYS161 | |
| D | LYS161 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor; specific for (S)-substrate epimerization => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS265 | |
| B | LYS265 | |
| C | LYS265 | |
| D | LYS265 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 36 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | THR134 | |
| B | THR134 | |
| B | LYS159 | |
| B | ASP188 | |
| B | ASN190 | |
| B | GLU216 | |
| B | ASP241 | |
| B | CYS292 | |
| B | ASP317 | |
| B | ASP319 | |
| C | THR134 | |
| A | LYS159 | |
| C | LYS159 | |
| C | ASP188 | |
| C | ASN190 | |
| C | GLU216 | |
| C | ASP241 | |
| C | CYS292 | |
| C | ASP317 | |
| C | ASP319 | |
| D | THR134 | |
| D | LYS159 | |
| A | ASP188 | |
| D | ASP188 | |
| D | ASN190 | |
| D | GLU216 | |
| D | ASP241 | |
| D | CYS292 | |
| D | ASP317 | |
| D | ASP319 | |
| A | ASN190 | |
| A | GLU216 | |
| A | ASP241 | |
| A | CYS292 | |
| A | ASP317 | |
| A | ASP319 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| A | ASP317 | |
| A | LYS161 | |
| A | LYS159 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| B | ASP317 | |
| B | LYS161 | |
| B | LYS159 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| C | ASP317 | |
| C | LYS161 | |
| C | LYS159 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| D | ASP317 | |
| D | LYS161 | |
| D | LYS159 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| A | LYS161 | |
| A | LYS265 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| B | LYS161 | |
| B | LYS265 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| C | LYS161 | |
| C | LYS265 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| D | LYS161 | |
| D | LYS265 |
