4LNO
B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: form two of GS-1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004356 | molecular_function | glutamine synthetase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006542 | biological_process | glutamine biosynthetic process |
| A | 0016595 | molecular_function | glutamate binding |
| A | 0016874 | molecular_function | ligase activity |
| A | 0043562 | biological_process | cellular response to nitrogen levels |
| A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070406 | molecular_function | glutamine binding |
| A | 0090295 | biological_process | nitrogen catabolite repression of transcription |
| A | 0140297 | molecular_function | DNA-binding transcription factor binding |
| A | 0140416 | molecular_function | transcription regulator inhibitor activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004356 | molecular_function | glutamine synthetase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006542 | biological_process | glutamine biosynthetic process |
| B | 0016595 | molecular_function | glutamate binding |
| B | 0016874 | molecular_function | ligase activity |
| B | 0043562 | biological_process | cellular response to nitrogen levels |
| B | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070406 | molecular_function | glutamine binding |
| B | 0090295 | biological_process | nitrogen catabolite repression of transcription |
| B | 0140297 | molecular_function | DNA-binding transcription factor binding |
| B | 0140416 | molecular_function | transcription regulator inhibitor activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004356 | molecular_function | glutamine synthetase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006542 | biological_process | glutamine biosynthetic process |
| C | 0016595 | molecular_function | glutamate binding |
| C | 0016874 | molecular_function | ligase activity |
| C | 0043562 | biological_process | cellular response to nitrogen levels |
| C | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0070406 | molecular_function | glutamine binding |
| C | 0090295 | biological_process | nitrogen catabolite repression of transcription |
| C | 0140297 | molecular_function | DNA-binding transcription factor binding |
| C | 0140416 | molecular_function | transcription regulator inhibitor activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004356 | molecular_function | glutamine synthetase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006542 | biological_process | glutamine biosynthetic process |
| D | 0016595 | molecular_function | glutamate binding |
| D | 0016874 | molecular_function | ligase activity |
| D | 0043562 | biological_process | cellular response to nitrogen levels |
| D | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0070406 | molecular_function | glutamine binding |
| D | 0090295 | biological_process | nitrogen catabolite repression of transcription |
| D | 0140297 | molecular_function | DNA-binding transcription factor binding |
| D | 0140416 | molecular_function | transcription regulator inhibitor activity |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004356 | molecular_function | glutamine synthetase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006542 | biological_process | glutamine biosynthetic process |
| E | 0016595 | molecular_function | glutamate binding |
| E | 0016874 | molecular_function | ligase activity |
| E | 0043562 | biological_process | cellular response to nitrogen levels |
| E | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0070406 | molecular_function | glutamine binding |
| E | 0090295 | biological_process | nitrogen catabolite repression of transcription |
| E | 0140297 | molecular_function | DNA-binding transcription factor binding |
| E | 0140416 | molecular_function | transcription regulator inhibitor activity |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0000287 | molecular_function | magnesium ion binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004356 | molecular_function | glutamine synthetase activity |
| F | 0005515 | molecular_function | protein binding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006542 | biological_process | glutamine biosynthetic process |
| F | 0016595 | molecular_function | glutamate binding |
| F | 0016874 | molecular_function | ligase activity |
| F | 0043562 | biological_process | cellular response to nitrogen levels |
| F | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0070406 | molecular_function | glutamine binding |
| F | 0090295 | biological_process | nitrogen catabolite repression of transcription |
| F | 0140297 | molecular_function | DNA-binding transcription factor binding |
| F | 0140416 | molecular_function | transcription regulator inhibitor activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 501 |
| Chain | Residue |
| A | GLU134 |
| A | GLU189 |
| A | GLU196 |
| A | GLN503 |
| A | HOH608 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 502 |
| Chain | Residue |
| B | GLU65 |
| A | GLU132 |
| A | HIS245 |
| A | GLU333 |
| A | HOH608 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GLN A 503 |
| Chain | Residue |
| A | GLU134 |
| A | TYR156 |
| A | GLU189 |
| A | GLN194 |
| A | GLY241 |
| A | HIS245 |
| A | ARG298 |
| A | GLU304 |
| A | MG501 |
| A | HOH608 |
| A | HOH609 |
| A | HOH663 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 501 |
| Chain | Residue |
| B | GLU134 |
| B | GLU189 |
| B | GLU196 |
| B | GLN503 |
| B | HOH686 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 502 |
| Chain | Residue |
| B | GLU132 |
| B | HIS245 |
| B | GLU333 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GLN B 503 |
| Chain | Residue |
| B | GLU134 |
| B | TYR156 |
| B | GLU189 |
| B | GLY241 |
| B | HIS245 |
| B | ARG298 |
| B | GLU304 |
| B | ALA305 |
| B | ARG335 |
| B | MG501 |
| B | HOH604 |
| C | HOH607 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GLN C 501 |
| Chain | Residue |
| C | GLU134 |
| C | TYR156 |
| C | GLU189 |
| C | GLY241 |
| C | HIS245 |
| C | ARG298 |
| C | GLU304 |
| C | MG503 |
| C | HOH603 |
| C | HOH628 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 502 |
| Chain | Residue |
| C | GLU132 |
| C | HIS245 |
| C | GLU333 |
| D | GLU65 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 503 |
| Chain | Residue |
| C | GLU134 |
| C | GLU189 |
| C | GLU196 |
| C | GLN501 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 501 |
| Chain | Residue |
| D | GLU134 |
| D | GLU189 |
| D | GLU196 |
| D | GLN503 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 502 |
| Chain | Residue |
| D | GLU132 |
| D | HIS245 |
| D | GLU333 |
| D | HOH704 |
| E | GLU65 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GLN D 503 |
| Chain | Residue |
| D | GLU134 |
| D | TYR156 |
| D | GLU189 |
| D | GLY241 |
| D | HIS245 |
| D | ARG298 |
| D | GLU304 |
| D | MG501 |
| D | HOH611 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG E 501 |
| Chain | Residue |
| E | GLU132 |
| E | HIS245 |
| E | GLU333 |
| E | HOH627 |
| F | GLU65 |
| F | HOH602 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG E 502 |
| Chain | Residue |
| E | GLU134 |
| E | GLU189 |
| E | GLU196 |
| E | GLN503 |
| site_id | BC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GLN E 503 |
| Chain | Residue |
| E | GLU134 |
| E | TYR156 |
| E | GLU189 |
| E | ASN240 |
| E | GLY241 |
| E | HIS245 |
| E | ARG298 |
| E | GLU304 |
| E | MG502 |
| E | HOH636 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG F 501 |
| Chain | Residue |
| F | HIS245 |
| F | GLU333 |
| F | GLU132 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG F 502 |
| Chain | Residue |
| F | GLU134 |
| F | GLU189 |
| F | GLU196 |
| F | GLN503 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GLN F 503 |
| Chain | Residue |
| F | GLU134 |
| F | GLU189 |
| F | GLY241 |
| F | HIS245 |
| F | ARG298 |
| F | GLU304 |
| F | MG502 |
| F | HOH612 |
| F | HOH659 |
Functional Information from PROSITE/UniProt
| site_id | PS00180 |
| Number of Residues | 19 |
| Details | GLNA_1 Glutamine synthetase signature 1. FDGSSiegfvrieESDmyL |
| Chain | Residue | Details |
| A | PHE52-LEU70 |
| site_id | PS00181 |
| Number of Residues | 16 |
| Details | GLNA_ATP Glutamine synthetase putative ATP-binding region signature. KPLfgv..NGSGmHcnlS |
| Chain | Residue | Details |
| A | LYS234-SER249 |
| site_id | PS00182 |
| Number of Residues | 13 |
| Details | GLNA_ADENYLATION Glutamine synthetase class-I adenylation site. KLeapapIDRNIY |
| Chain | Residue | Details |
| A | LYS361-TYR373 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 510 |
| Details | Domain: {"description":"GS beta-grasp","evidences":[{"source":"PROSITE-ProRule","id":"PRU01330","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2016 |
| Details | Domain: {"description":"GS catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU01331","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24158439","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25691471","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LNF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LNI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LNK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LNN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4S0R","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24158439","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25691471","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LNF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LNI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LNK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4S0R","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P9WN39","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24158439","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25691471","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LNF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LNK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LNN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4S0R","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24158439","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25691471","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LNF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LNK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4S0R","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P77961","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A1P6","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 6 |
| Details | Site: {"description":"Important for inhibition by glutamine","evidences":[{"source":"PubMed","id":"24158439","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






