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2JAG

L1-intermediate of halorhodopsin T203V

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0007602biological_processphototransduction
A0009881molecular_functionphotoreceptor activity
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00327
Number of Residues12
DetailsBACTERIAL_OPSIN_RET Bacterial rhodopsins retinal binding site. YSVLDVfAKyVF
ChainResidueDetails
ATYR234-PHE245

site_idPS00950
Number of Residues13
DetailsBACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYlTWaLSTPMIL
ChainResidueDetails
AARG108-LEU120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues37
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:10827943
ChainResidueDetails
AALA22-GLU25
ASER82-GLN105
ATHR155-ALA157
AGLY217-SER226

site_idSWS_FT_FI2
Number of Residues25
DetailsTRANSMEM: Helical; Name=Helix A
ChainResidueDetails
AASN26-GLY51

site_idSWS_FT_FI3
Number of Residues36
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:10827943
ChainResidueDetails
AARG52-GLY57
AASP128-ASP130
ATHR181-THR192
AASN256-ASP274

site_idSWS_FT_FI4
Number of Residues23
DetailsTRANSMEM: Helical; Name=Helix B
ChainResidueDetails
AARG58-LEU81

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=Helix C
ChainResidueDetails
ATRP106-ALA127

site_idSWS_FT_FI6
Number of Residues23
DetailsTRANSMEM: Helical; Name=Helix D
ChainResidueDetails
ALEU131-THR154

site_idSWS_FT_FI7
Number of Residues22
DetailsTRANSMEM: Helical; Name=Helix E
ChainResidueDetails
ALEU158-VAL180

site_idSWS_FT_FI8
Number of Residues23
DetailsTRANSMEM: Helical; Name=Helix F
ChainResidueDetails
AALA193-VAL216

site_idSWS_FT_FI9
Number of Residues28
DetailsTRANSMEM: Helical; Name=Helix G
ChainResidueDetails
AVAL227-ASN255

site_idSWS_FT_FI10
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:10827943, ECO:0000269|PubMed:17117890
ChainResidueDetails
AGLN105
ATHR111
ASER115

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: N6-(retinylidene)lysine
ChainResidueDetails
ALYS242

220113

PDB entries from 2024-05-22

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