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5N1T

Crystal structure of complex between flavocytochrome c and copper chaperone CopC from T. paradoxus

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0050660molecular_functionflavin adenine dinucleotide binding
B0009055molecular_functionelectron transfer activity
B0020037molecular_functionheme binding
M0005507molecular_functioncopper ion binding
M0042597cellular_componentperiplasmic space
M0046688biological_processresponse to copper ion
W0005507molecular_functioncopper ion binding
W0042597cellular_componentperiplasmic space
W0046688biological_processresponse to copper ion
Functional Information from PDB Data
site_idAC1
Number of Residues29
Detailsbinding site for residue FAD A 501
ChainResidue
AGLY40
ATRP108
AVAL109
ASER135
APRO136
AGLY137
ATRP160
AARG192
ACSS193
AILE288
AGLY320
AGLY42
AASP321
ALYS330
AALA331
AGLY332
APHE333
AALA335
ATYR365
ATRP415
AHOH610
AHOH614
APHE43
AGLY44
AASN65
APRO66
ATYR70
ACYS73
APRO74

site_idAC2
Number of Residues21
Detailsbinding site for residue HEC B 901
ChainResidue
APHE333
ATHR363
ATYR411
BCYS11
BCYS14
BHIS15
BILE25
BLEU28
BILE36
BTHR39
BMET40
BPHE43
BARG48
BSER50
BTHR51
BVAL52
BMET53
BGLN56
BTYR60
BILE68
BHOH1001

site_idAC3
Number of Residues3
Detailsbinding site for residue CU W 201
ChainResidue
WHIS1
WASP110
WHIS112

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL W 202
ChainResidue
WASP32
WARG33
WSER35
WTHR36

Functional Information from PROSITE/UniProt
site_idPS00482
Number of Residues9
DetailsDIHYDROOROTASE_1 Dihydroorotase signature 1. DAHAHLRaA
ChainResidueDetails
MASP-1-ALA7

246031

PDB entries from 2025-12-10

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