Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3AYM

Crystal structure of the batho intermediate of squid rhodopsin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0005886cellular_componentplasma membrane
A0007186biological_processG protein-coupled receptor signaling pathway
A0007601biological_processvisual perception
A0007602biological_processphototransduction
A0008020molecular_functionG protein-coupled photoreceptor activity
A0009584biological_processdetection of visible light
A0009881molecular_functionphotoreceptor activity
A0016020cellular_componentmembrane
A0016918molecular_functionretinal binding
A0033583cellular_componentrhabdomere membrane
A0042995cellular_componentcell projection
A0071482biological_processcellular response to light stimulus
B0004930molecular_functionG protein-coupled receptor activity
B0005886cellular_componentplasma membrane
B0007186biological_processG protein-coupled receptor signaling pathway
B0007601biological_processvisual perception
B0007602biological_processphototransduction
B0008020molecular_functionG protein-coupled photoreceptor activity
B0009584biological_processdetection of visible light
B0009881molecular_functionphotoreceptor activity
B0016020cellular_componentmembrane
B0016918molecular_functionretinal binding
B0033583cellular_componentrhabdomere membrane
B0042995cellular_componentcell projection
B0071482biological_processcellular response to light stimulus
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. MSImTMAMISIDRYNvI
ChainResidueDetails
AMET121-ILE137

site_idPS00238
Number of Residues17
DetailsOPSIN Visual pigments (opsins) retinal binding site. LPvMfAKASAihNPmiY
ChainResidueDetails
ALEU299-TYR315

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues154
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:18463093, ECO:0000269|PubMed:18480818, ECO:0000269|PubMed:21906602, ECO:0000269|PubMed:26024518
ChainResidueDetails
AGLY2-VAL33
ALEU98-LYS109
AGLY173-SER199
AALA284-THR293
BGLY2-VAL33
BLEU98-LYS109
BGLY173-SER199
BALA284-THR293

site_idSWS_FT_FI2
Number of Residues48
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:18463093, ECO:0000269|PubMed:18480818, ECO:0000269|PubMed:21906602, ECO:0000269|PubMed:26024518
ChainResidueDetails
ATYR34-LEU58
BTYR34-LEU58

site_idSWS_FT_FI3
Number of Residues396
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:18463093, ECO:0000269|PubMed:18480818, ECO:0000269|PubMed:21906602, ECO:0000269|PubMed:26024518
ChainResidueDetails
APHE59-ASN70
AASP132-ARG151
AMET225-LYS261
ASER316-ALA448
BPHE59-ASN70
BASP132-ARG151
BMET225-LYS261
BSER316-ALA448

site_idSWS_FT_FI4
Number of Residues52
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:18463093, ECO:0000269|PubMed:18480818, ECO:0000269|PubMed:21906602, ECO:0000269|PubMed:26024518
ChainResidueDetails
AMET71-PHE97
BMET71-PHE97

site_idSWS_FT_FI5
Number of Residues42
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:18463093, ECO:0000269|PubMed:18480818, ECO:0000269|PubMed:21906602, ECO:0000269|PubMed:26024518
ChainResidueDetails
AVAL110-ILE131
BVAL110-ILE131

site_idSWS_FT_FI6
Number of Residues40
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:18463093, ECO:0000269|PubMed:18480818, ECO:0000269|PubMed:21906602, ECO:0000269|PubMed:26024518
ChainResidueDetails
AALA152-PHE172
BALA152-PHE172

site_idSWS_FT_FI7
Number of Residues48
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:18463093, ECO:0000269|PubMed:18480818, ECO:0000269|PubMed:21906602, ECO:0000269|PubMed:26024518
ChainResidueDetails
AASN200-VAL224
BASN200-VAL224

site_idSWS_FT_FI8
Number of Residues42
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:18463093, ECO:0000269|PubMed:18480818, ECO:0000269|PubMed:21906602, ECO:0000269|PubMed:26024518
ChainResidueDetails
AILE262-LEU283
BILE262-LEU283

site_idSWS_FT_FI9
Number of Residues42
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:18463093, ECO:0000269|PubMed:18480818, ECO:0000269|PubMed:21906602, ECO:0000269|PubMed:26024518
ChainResidueDetails
APRO294-TYR315
BPRO294-TYR315

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-(retinylidene)lysine => ECO:0000269|PubMed:18463093, ECO:0000269|PubMed:18480818, ECO:0000269|PubMed:21906602, ECO:0000269|PubMed:26024518, ECO:0000269|PubMed:3191148, ECO:0007744|PDB:2Z73, ECO:0007744|PDB:4WW3
ChainResidueDetails
ALYS305
BLYS305

site_idSWS_FT_FI11
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:18463093, ECO:0007744|PDB:2ZIY
ChainResidueDetails
ACYS336
BCYS336

site_idSWS_FT_FI12
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:18463093, ECO:0000269|PubMed:18480818, ECO:0007744|PDB:2ZIY
ChainResidueDetails
ACYS337
BCYS337

site_idSWS_FT_FI13
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:18463093
ChainResidueDetails
AASN8
BASN8

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon