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

3MG3

Crystal structure of the orange carotenoid protein R155L mutant from cyanobacteria synechocystis sp. PCC 6803

Replaces:  3I1X
Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0009579cellular_componentthylakoid
A0009881molecular_functionphotoreceptor activity
A0016020cellular_componentmembrane
A0016037biological_processlight absorption
A0030089cellular_componentphycobilisome
A0031404molecular_functionchloride ion binding
A0031676cellular_componentplasma membrane-derived thylakoid membrane
B0005515molecular_functionprotein binding
B0009579cellular_componentthylakoid
B0009881molecular_functionphotoreceptor activity
B0016020cellular_componentmembrane
B0016037biological_processlight absorption
B0030089cellular_componentphycobilisome
B0031404molecular_functionchloride ion binding
B0031676cellular_componentplasma membrane-derived thylakoid membrane
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ECH A 351
ChainResidue
AILE40
ALEU205
ACYS245
AVAL273
AMET284
ATRP288
AILE303
AGOL326
ATYR44
ATRP110
ATYR111
AGLY114
AILE151
ATHR152
AVAL158
ATYR201

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ECH B 351
ChainResidue
BILE40
BTYR44
BLEU107
BTRP110
BTYR111
BGLY114
BILE151
BTHR152
BVAL158
BTYR201
BLEU205
BCYS245
BVAL273
BMET284
BTRP288
BILE303
BGOL326

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 324
ChainResidue
AALA55
APRO56
AGLY57
AGLU174
APRO276
ATRP277
AHOH1011
AHOH1088
AHOH1174
AHOH1376

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 325
ChainResidue
AASN104
AGLU244
ATRP277
AGOL326
AHOH1012
AHOH1019

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B 324
ChainResidue
BALA55
BPRO56
BGLY57
BGLU174
BPRO276
BTRP277
BHOH1010
BHOH1059
BHOH1077
BHOH1171

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 325
ChainResidue
BASN104
BGLU244
BTRP277
BGOL326
BHOH1009
BHOH1023

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 326
ChainResidue
APRO225
APRO226
AGLN228
APHE240
AGOL325
AECH351
AHOH1184
AHOH1462
AHOH1646

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 326
ChainResidue
BASN156
BPRO225
BPRO226
BGLN228
BPHE240
BGOL325
BECH351
BHOH1226
BHOH1485

site_idAC9
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GOL B 327
ChainResidue
ASER132
AASN134
BARG9
BGLY10
BILE11
BPHE12
BPRO13
BTHR15
BARG289
BHOH1035
BHOH1097
BHOH1134
BHOH1469

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: only in form RCP => ECO:0000269|PubMed:26113721
ChainResidueDetails
AGLU34
ATHR80
AILE125
BGLU34
BTHR80
BILE125

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: in forms OCP and RCP => ECO:0000269|PubMed:20368334, ECO:0000269|PubMed:26113721
ChainResidueDetails
ALEU37
ALEU107
BLEU37
BLEU107

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: residues alter contact in forms OCP and RCP => ECO:0000269|PubMed:20368334, ECO:0000269|PubMed:26113721
ChainResidueDetails
AILE151
BILE151

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: only in form OCP => ECO:0000269|PubMed:20368334, ECO:0000269|PubMed:26113721
ChainResidueDetails
ATYR201
ACYS245
AVAL273
ATRP288
BTYR201
BCYS245
BVAL273
BTRP288

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon