Online Services

●I-TASSER ●I-TASSER-MTD ●C-I-TASSER ●CR-I-TASSER ●QUARK ●C-QUARK ●LOMETS ●MUSTER ●CEthreader ●SEGMER ●DeepFold ●DeepFoldRNA ●FoldDesign ●COFACTOR ●COACH ●MetaGO ●TripletGO ●IonCom ●FG-MD ●ModRefiner ●REMO ●DEMO ●DEMO-EM ●SPRING ●COTH ●Threpp ●PEPPI ●BSpred ●ANGLOR ●EDock ●BSP-SLIM ●SAXSTER ●FUpred ●ThreaDom ●ThreaDomEx ●EvoDesign ●BindProf ●BindProfX ●SSIPe ●GPCR-I-TASSER ●MAGELLAN ●ResQ ●STRUM ●DAMpred

●TM-score ●TM-align ●US-align ●MM-align ●RNA-align ●NW-align ●LS-align ●EDTSurf ●MVP ●MVP-Fit ●SPICKER ●HAAD ●PSSpred ●3DRobot ●MR-REX ●I-TASSER-MR ●SVMSEQ ●NeBcon ●ResPRE ●TripletRes ●DeepPotential ●WDL-RF ●ATPbind ●DockRMSD ●DeepMSA ●FASPR ●EM-Refiner ●GPU-I-TASSER

●BioLiP ●E. coli ●GLASS ●GPCR-HGmod ●GPCR-RD ●GPCR-EXP ●Tara-3D ●TM-fold ●DECOYS ●POTENTIAL ●RW/RWplus ●EvoEF ●HPSF ●THE-DB ●ADDRESS ●Alpaca-Antibody ●CASP7 ●CASP8 ●CASP9 ●CASP10 ●CASP11 ●CASP12 ●CASP13 ●CASP14

Structure of PDB 5b5m Chain C

Receptor sequence >5b5mC (length=317) Species: 1050 (Thermochromatium tepidum) [Search protein sequence] SVMLLGCEGPPPGTEQIGYRGVGMENYYNKRQRALSIQANQPVESLPAAD STGPKASEVYQNVQVLKDLSVGEFTRTMVAVTTWVSPKEGCNYCHVPGNW ASDDIYTKVVSRRMFELVRAANSDWKAHVAETGVTCYTCHRGNPVPKYAW VTDPGPKYPSGLKPTGQNYGSKTVAYASLPFDPLTPFLDQANEIRITGNA ALAGSNPASLKQAEWTFGLMMNISDSLGVGCTFCHNTRAFNDWTQSTPKR TTAWYAIRHVRDINQNYIWPLNDVLPASRKGPYGDPLRVSCMTCHQAVNK PLYGAQMAKDYPGLYKT

3D structure PDB 5b5m Structural Basis for the Unusual Qy Red-Shift and Enhanced Thermostability of the LH1 Complex from Thermochromatium tepidum. Chain C Resolution 3.3 Å 3D structure [Spin on] [Spin off] [Reset orientation] [High quality] [Low quality] [White background] [Black background] [Download] [Download structure with residue number starting from 1]

Enzymatic activity Enzyme Commision number ?

Interaction with ligand Site # Ligand Ligand chain Binding residues on receptor (original residue number in PDB) Binding residues on receptor (residue number reindexed from 1) Binding affinity BS01 HEM C Y76 Q77 N78 Q80 V81 F90 M94 V97 T98 C107 C110 H111 W116 A117 K124 S127 R128 Y60 Q61 N62 Q64 V65 F74 M78 V81 T82 C91 C94 H95 W100 A101 K108 S111 R112 BS02 HEM C V101 Y122 V126 M130 L133 V134 C152 C155 H156 V161 P162 R295 L303 R304 V305 V85 Y106 V110 M114 L117 V118 C136 C139 H140 V145 P146 R279 L287 R288 V289 BS03 HEM C R211 I212 T213 T232 F233 M236 I239 S240 C247 C250 H251 F256 N257 R266 W270 R274 R195 I196 T197 T216 F217 M220 I223 S224 C231 C234 H235 F240 N241 R250 W254 R258 BS04 HEM C H144 A146 T148 V150 L243 K265 T268 A269 A272 I273 C307 C310 H311 N315 K316 P317 H128 A130 T132 V134 L227 K249 T252 A253 A256 I257 C291 C294 H295 N299 K300 P301

Gene Ontology Molecular Function GO:0005506 iron ion binding GO:0009055 electron transfer activity GO:0020037 heme binding

	Biological Process
GO:0019684	photosynthesis, light reaction

	Cellular Component
GO:0030077	plasma membrane light-harvesting complex

View graph for Molecular Function

View graph for Biological Process

View graph for Cellular Component