Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6FFI

Crystal Structure of mGluR5 in complex with MMPEP at 2.2 A

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0004930molecular_functionG protein-coupled receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue OLA A 4001
ChainResidue
AASN897
AVAL901
ALEU904
ALEU912
ACYS942
ATRP945
APHE953

site_idAC2
Number of Residues4
Detailsbinding site for residue OLA A 4002
ChainResidue
AVAL570
AOLA4004
ASER568
APRO569

site_idAC3
Number of Residues5
Detailsbinding site for residue OLA A 4003
ChainResidue
ATYR645
AILE649
APHE872
AILE873
AOLA4005

site_idAC4
Number of Residues5
Detailsbinding site for residue OLA A 4004
ChainResidue
APRO569
ACYS588
AILE636
AOLA4002
AHOH4130

site_idAC5
Number of Residues2
Detailsbinding site for residue OLA A 4005
ChainResidue
ATYR645
AOLA4003

site_idAC6
Number of Residues9
Detailsbinding site for residue MES A 4006
ChainResidue
ATYR816
ATYR890
AASN956
ATYR957
ALYS958
AILE959
AHOH4105
AHOH4176
AHOH4182

site_idAC7
Number of Residues2
Detailsbinding site for residue OLA A 4007
ChainResidue
AARG574
AILE581

site_idAC8
Number of Residues1
Detailsbinding site for residue OLA A 4008
ChainResidue
ATHR598

site_idAC9
Number of Residues10
Detailsbinding site for residue D8B A 4009
ChainResidue
AGLY624
ASER654
APRO655
ASER658
ATYR659
AILE944
ATRP945
APHE948
ASER965
ASER969

Functional Information from PROSITE/UniProt
site_idPS00981
Number of Residues11
DetailsG_PROTEIN_RECEP_F3_3 G-protein coupled receptors family 3 signature 3. FNEAKyIAFTM
ChainResidueDetails
APHE928-MET938

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1892846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=1"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues21
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"25042998","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues9
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"25042998","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=3"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=4"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=5"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=6"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=7"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
ALEU692proton shuttle (general acid/base)
ATYR701covalent catalysis

238895

PDB entries from 2025-07-16

PDB statisticsPDBj update infoContact PDBjnumon