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5KKH

2.1-Angstrom In situ Mylar structure of bacteriorhodopsin from Haloquadratum walsbyi (HwBR) at 100 K

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
A1902600biological_processproton transmembrane transport
B0005216molecular_functionmonoatomic ion channel activity
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0007602biological_processphototransduction
B0009881molecular_functionphotoreceptor activity
B0016020cellular_componentmembrane
B1902600biological_processproton transmembrane transport
C0005216molecular_functionmonoatomic ion channel activity
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0007602biological_processphototransduction
C0009881molecular_functionphotoreceptor activity
C0016020cellular_componentmembrane
C1902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue OLC A 301
ChainResidue
AGLU48
BGLY117
BALA118
BPHE125
BVAL128
BOLC301
AVAL51
AILE52
ALEU55
AILE59
AALA89
ALEU103
AOLC303
BARG114

site_idAC2
Number of Residues10
Detailsbinding site for residue OLB A 302
ChainResidue
AILE122
APHE125
APHE155
ATYR159
CTHR24
CILE35
CVAL51
CLEU55
CALA61
CHOH423

site_idAC3
Number of Residues6
Detailsbinding site for residue OLC A 303
ChainResidue
APRO99
ALEU103
ALEU107
AGLN113
AILE116
AOLC301

site_idAC4
Number of Residues11
Detailsbinding site for residue RET A 304
ChainResidue
ATRP94
ATHR97
ATHR98
AMET126
ATRP146
ASER149
ATHR150
ATRP190
ATYR193
AALA223
ALYS224

site_idAC5
Number of Residues5
Detailsbinding site for residue OLC B 301
ChainResidue
AOLC301
BLEU100
BGLN113
BILE116
BALA124

site_idAC6
Number of Residues7
Detailsbinding site for residue OLC B 302
ChainResidue
BVAL154
BLEU157
BTYR158
BVAL161
BALA162
BGLY165
BGLU166

site_idAC7
Number of Residues16
Detailsbinding site for residue OLB B 303
ChainResidue
BTHR24
BLEU28
BMET31
BLYS47
BILE54
BLEU55
BALA58
BLEU65
BHOH403
BHOH421
CILE122
CPHE125
CILE148
CSER152
CPHE155
CTYR159

site_idAC8
Number of Residues8
Detailsbinding site for residue OLC C 301
ChainResidue
BPHE96
CLEU95
CPRO99
CLEU107
CALA111
CSER112
CGLN113
COLB303

site_idAC9
Number of Residues9
Detailsbinding site for residue OLC C 302
ChainResidue
BGLU48
BVAL51
BILE59
CARG114
CASP115
CGLY117
CALA118
CALA124
CVAL128

site_idAD1
Number of Residues11
Detailsbinding site for residue OLB C 303
ChainResidue
AGLY117
AGLY121
AVAL128
CGLU48
CILE59
CPHE96
CLEU100
CLEU103
COLC301
CHOH414
CHOH415

Functional Information from PROSITE/UniProt
site_idPS00327
Number of Residues12
DetailsBACTERIAL_OPSIN_RET Bacterial rhodopsins retinal binding site. FMVLDLvAKvGF
ChainResidueDetails
APHE216-PHE227

site_idPS00950
Number of Residues13
DetailsBACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYaDWlFTTPLLL
ChainResidueDetails
AARG90-LEU102

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues420
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AGLU16-ALA36
BTYR91-ALA111
BILE116-THR136
BALA144-PHE164
BILE185-ALA205
BGLU212-LEU232
CGLU16-ALA36
CVAL51-PHE71
CTYR91-ALA111
CILE116-THR136
CALA144-PHE164
AVAL51-PHE71
CILE185-ALA205
CGLU212-LEU232
ATYR91-ALA111
AILE116-THR136
AALA144-PHE164
AILE185-ALA205
AGLU212-LEU232
BGLU16-ALA36
BVAL51-PHE71

site_idSWS_FT_FI2
Number of Residues3
DetailsSITE: Primary proton acceptor => ECO:0000250
ChainResidueDetails
AASP93
BASP93
CASP93

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000250
ChainResidueDetails
AGLN7
BGLN7
CGLN7

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: N6-(retinylidene)lysine => ECO:0000250
ChainResidueDetails
ALYS224
BLYS224
CLYS224

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PDB entries from 2024-07-17

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