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4Y9J

Crystal Structure of Caenorhabditis elegans ACDH-11 in complex with C11-CoA

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003995molecular_functionacyl-CoA dehydrogenase activity
A0005504molecular_functionfatty acid binding
A0006631biological_processfatty acid metabolic process
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A1990845biological_processadaptive thermogenesis
B0000166molecular_functionnucleotide binding
B0003995molecular_functionacyl-CoA dehydrogenase activity
B0005504molecular_functionfatty acid binding
B0006631biological_processfatty acid metabolic process
B0016491molecular_functionoxidoreductase activity
B0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
B1990845biological_processadaptive thermogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues37
Detailsbinding site for residue FAD A 701
ChainResidue
AGLN206
ALYS295
ATHR298
ATRP463
AGLU464
ATHR466
AASN468
AVAL469
ALEU472
AUCC702
AHOH811
AMET208
AHOH813
AHOH820
AHOH873
AHOH877
AHOH995
AHOH1035
AHOH1043
AHOH1045
BARG359
BVAL361
ATHR209
BPHE362
BGLN366
BHIS372
BGLU437
BCYS438
BGLY440
BGLY441
BHOH894
AGLY213
AGLY214
ASER215
APHE241
ASER242
ASER243

site_idAC2
Number of Residues29
Detailsbinding site for residue UCC A 702
ChainResidue
ASER161
ACYS162
AGLN206
AMET208
ATHR209
AGLY214
ASER215
AALA218
ASER267
AARG321
AVAL323
ASER327
ALEU330
AASN331
AARG334
AASN337
AALA340
ATRP463
AGLU464
AGLY465
AASP473
AFAD701
AHOH801
AHOH803
AHOH821
AHOH823
AHOH885
AHOH904
AHOH917

site_idAC3
Number of Residues37
Detailsbinding site for residue FAD B 701
ChainResidue
BHOH1011
BHOH1022
BHOH1044
BHOH1109
AARG359
AVAL361
APHE362
AGLN366
ATRP369
AHIS372
AGLU437
ACYS438
AGLY440
AGLY441
AHOH815
BGLN206
BMET208
BTHR209
BGLY214
BSER215
BPHE241
BSER242
BSER243
BLYS295
BTHR298
BILE462
BTRP463
BTHR466
BASN468
BVAL469
BLEU472
BUCC702
BHOH827
BHOH861
BHOH927
BHOH1001
BHOH1002

site_idAC4
Number of Residues28
Detailsbinding site for residue UCC B 702
ChainResidue
BSER161
BALA165
BGLN206
BSER215
BALA218
BSER267
BARG321
BSER327
BLEU330
BASN331
BARG334
BALA340
BARG414
BTRP463
BGLU464
BGLY465
BVAL469
BARG476
BFAD701
BHOH825
BHOH829
BHOH844
BHOH872
BHOH889
BHOH896
BHOH946
BHOH966
BHOH996

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: in other chain => ECO:0007744|PDB:4Y9J, ECO:0007744|PDB:4Y9L
ChainResidueDetails
ASER215
AALA250
ATHR375
AASP473
BSER215
BALA250
BTHR375
BASP473

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0007744|PDB:4Y9J
ChainResidueDetails
ATYR224
ALYS276
AGLY343
BTYR224
BLYS276
BGLY343

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:4Y9J, ECO:0007744|PDB:4Y9L
ChainResidueDetails
ALYS368
ALEU450
BLYS368
BLEU450

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:4Y9L
ChainResidueDetails
AGLU446
BGLU446

226707

PDB entries from 2024-10-30

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