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3OZ2

Crystal structure of a geranylgeranyl bacteriochlorophyll reductase-like (Ta0516) from Thermoplasma acidophilum at 1.60 A resolution

Replaces:  3CGV
Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0006650biological_processglycerophospholipid metabolic process
A0008654biological_processphospholipid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016628molecular_functionoxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
A0045550molecular_functiongeranylgeranyl reductase activity
A0046467biological_processmembrane lipid biosynthetic process
A0050660molecular_functionflavin adenine dinucleotide binding
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
A0071949molecular_functionFAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues37
DetailsBINDING SITE FOR RESIDUE FAD A 501
ChainResidue
AGLY10
AGLY45
AGLU46
AGLY47
AARG100
APRO123
AALA124
AALA156
AASP157
AGLY158
AGLU162
AGLY12
APHE213
AVAL264
AGLY282
AASP283
AGLY294
AGLY295
AILE296
AALA299
AOZ2502
AHOH517
APRO13
AHOH518
AHOH524
AHOH528
AHOH622
AHOH623
AHOH628
AHOH630
AHOH687
AGLY14
AGLU33
ALYS34
AARG35
AARG43
ACYS44

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE OZ2 A 502
ChainResidue
ASER49
ATYR209
ATRP211
APRO290
AILE291
ATHR292
AGLY293
ALYS338
ALEU349
AILE372
ASER373
AVAL374
AFAD501
AEDO508
AGOL515
AHOH655
AHOH805
AHOH836

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 503
ChainResidue
AVAL118
ATRP119
AVAL120
AHIS141
AHOH575
AHOH790

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 504
ChainResidue
ALYS138
AGLU312
AGLU315
AHOH616

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 505
ChainResidue
AGLY132
ALYS133
AVAL134
AMSE275
AHOH585

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 506
ChainResidue
ATYR4
AHOH670
AHOH747

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 507
ChainResidue
AASN177
ASER227
ALYS346
AGLU347
AHOH617
AHOH785

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 508
ChainResidue
AASP289
ATHR292
AGLY294
AASN298
AOZ2502
AEDO509

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 509
ChainResidue
AASN298
AVAL301
AARG334
ALYS338
AEDO508
AHOH666

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 510
ChainResidue
AASP117
ATRP119
AHOH635

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 511
ChainResidue
AHOH558
AHOH684
AHOH769
AHOH788

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 512
ChainResidue
ALEU27
AHOH557
AHOH633
AHOH705
AALA23

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 513
ChainResidue
AGLY254
ALYS270
AMSE271
AHOH589
AHOH626
AHOH672
AHOH765

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 514
ChainResidue
APRO272
ATHR274
AMSE275
APRO321
AMSE324
AGLN325
AGLU328
AHOH604

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 515
ChainResidue
AGLY47
ALEU48
ASER49
AVAL69
ATHR197
AOZ2502

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues13
DetailsBINDING: BINDING => ECO:0000269|PubMed:20869368
ChainResidueDetails
AARG100
AALA124
AGLU162
AGLY208
AASP283
AILE291
AGLY295
ALYS338
AILE372
AGLY10
AGLU33
ACYS44
ASER49

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PDB entries from 2024-05-29

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