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2CFG

AGAO in complex with wc4d3 (Ru-wire inhibitor, 4-carbon linker, delta enantiomer, data set 3)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0008131molecular_functionprimary methylamine oxidase activity
A0009308biological_processamine metabolic process
A0016491molecular_functionoxidoreductase activity
A0016641molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
A0046872molecular_functionmetal ion binding
A0048038molecular_functionquinone binding
B0005507molecular_functioncopper ion binding
B0008131molecular_functionprimary methylamine oxidase activity
B0009308biological_processamine metabolic process
B0016491molecular_functionoxidoreductase activity
B0016641molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
B0046872molecular_functionmetal ion binding
B0048038molecular_functionquinone binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU A1628
ChainResidue
AHIS431
AHIS433
AHIS592
AHOH2198
AHOH2229

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A1629
ChainResidue
AHOH2235
AASP440
AMET441
AASP581
AILE582

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SO4 B1628
ChainResidue
AGLY350
AARG367
BASP316
BCYS317
BLEU318
BHIS345
BGOL1638
BHOH2231
BHOH2254
BHOH2424
BHOH2425
BHOH2426

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU B1630
ChainResidue
BHIS431
BHIS433
BHIS592
BHOH2252
BHOH2282

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B1631
ChainResidue
BASP440
BMET441
BASP581
BILE582
BHOH2287

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 B1633
ChainResidue
AASP316
ACYS317
ALEU318
AHIS345
AHOH2200
BGLY350
BARG367
BHOH2428
BHOH2429
BHOH2430

site_idAC7
Number of Residues16
DetailsBINDING SITE FOR RESIDUE R4A A1630
ChainResidue
AGLU102
APHE105
AALA135
APRO136
ALEU137
ATRP168
ATYR296
ATYR302
ATYR307
AGLY380
AASN381
ATPQ382
APHE407
BSER356
BASP357
BLEU358

site_idAC8
Number of Residues16
DetailsBINDING SITE FOR RESIDUE R4A B1632
ChainResidue
ASER356
AASP357
ALEU358
BGLU102
BPHE105
BALA135
BPRO136
BLEU137
BTRP168
BTYR296
BTYR302
BTYR307
BGLY380
BASN381
BTPQ382
BPHE407

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A1631
ChainResidue
AASN126
AASP161
AVAL197
AALA199
AHOH2361
AHOH2362
AHOH2363

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A1632
ChainResidue
ALEU590
AASP605
ATHR606
AHOH2341
BLYS610
BARG612

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A1633
ChainResidue
AASP444
AGLY445
APHE446
ATHR447
AASN499

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A1634
ChainResidue
AHOH2365
BHOH2408
AASN368
ATYR391
AASP393
ALYS610
AHOH2195
AHOH2205
AHOH2364

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B1629
ChainResidue
AGLU347
AARG370
ALYS401
AHOH2201
AHOH2208
BTRP349
BGLY350
BHOH2427

site_idBC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B1634
ChainResidue
BARG532
BARG533
BTHR554
BPHE557
BHIS561
BSER562
BGLY563
BGLY564
BALA565
BHOH2374

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B1635
ChainResidue
BASN126
BASP161
BVAL197
BALA199
BHOH2431
BHOH2432
BHOH2433

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B1636
ChainResidue
AARG612
BLEU590
BASP605
BTHR606
BHOH2434

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B1637
ChainResidue
BASP444
BGLY445
BPHE446
BTHR447
BASN499

site_idBC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B1638
ChainResidue
ATRP349
AGLY350
BGLU347
BARG370
BLYS401
BSO41628
BHOH2255
BHOH2262
BHOH2435

site_idCC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B1639
ChainResidue
BASN368
BTYR391
BASP393
BLYS610
BHOH2246
BHOH2260
BHOH2436
BHOH2437
BHOH2438

Functional Information from PROSITE/UniProt
site_idPS01164
Number of Residues14
DetailsCOPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. MVIsfftTigNYDY
ChainResidueDetails
AMET371-TYR384

site_idPS01165
Number of Residues14
DetailsCOPPER_AMINE_OXID_2 Copper amine oxidase copper-binding site signature. TfGltHFprvEDwP
ChainResidueDetails
ATHR587-PRO600

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P12807
ChainResidueDetails
AASP298
BASP298

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Schiff-base intermediate with substrate; via topaquinone => ECO:0000250|UniProtKB:P12807
ChainResidueDetails
ATPQ382
BTPQ382

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P12807
ChainResidueDetails
ATYR296
BTYR296

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P46883
ChainResidueDetails
AILE379
BILE379

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:9405045, ECO:0007744|PDB:1AV4, ECO:0007744|PDB:1AVL, ECO:0007744|PDB:1IU7, ECO:0007744|PDB:1IVU, ECO:0007744|PDB:1IVV, ECO:0007744|PDB:1IVW, ECO:0007744|PDB:1IVX, ECO:0007744|PDB:1RJO, ECO:0007744|PDB:1SIH, ECO:0007744|PDB:1SII, ECO:0007744|PDB:1UI8, ECO:0007744|PDB:1W4N, ECO:0007744|PDB:1W5Z, ECO:0007744|PDB:1W6C, ECO:0007744|PDB:1W6G, ECO:0007744|PDB:2BT3, ECO:0007744|PDB:2CFD, ECO:0007744|PDB:2CFG, ECO:0007744|PDB:2CFK, ECO:0007744|PDB:2CFL, ECO:0007744|PDB:2CFW, ECO:0007744|PDB:2CG0, ECO:0007744|PDB:2CG1, ECO:0007744|PDB:2CWT, ECO:0007744|PDB:2CWU, ECO:0007744|PDB:2CWV, ECO:0007744|PDB:2D1W, ECO:0007744|PDB:2E2T, ECO:0007744|PDB:2E2U, ECO:0007744|PDB:2E2V, ECO:0007744|PDB:2YX9, ECO:0007744|PDB:2ZL8, ECO:0007744|PDB:3AMO, ECO:0007744|PDB:3KII, ECO:0007744|PDB:3KN4, ECO:0007744|PDB:3WA2, ECO:0007744|PDB:3WA3
ChainResidueDetails
AHIS431
AHIS433
AHIS592
BHIS431
BHIS433
BHIS592

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: 2',4',5'-topaquinone => ECO:0000269|PubMed:9405045
ChainResidueDetails
ATPQ382
BTPQ382

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oac
ChainResidueDetails
AASP298

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oac
ChainResidueDetails
BASP298

237992

PDB entries from 2025-06-25

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