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5ZP0

Copper amine oxidase from Arthrobacter globiformis anaerobically reduced by ethylamine at pH 8 at 288 K (2)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0008131molecular_functionprimary amine oxidase activity
A0009308biological_processamine metabolic process
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
A0048038molecular_functionquinone binding
A0052595molecular_functionaliphatic amine oxidase activity
B0005507molecular_functioncopper ion binding
B0008131molecular_functionprimary amine oxidase activity
B0009308biological_processamine metabolic process
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
B0048038molecular_functionquinone binding
B0052595molecular_functionaliphatic amine oxidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CU A 701
ChainResidue
ATYQ382
AHIS431
AHIS433
AHIS592
AHOH935
AHOH988

site_idAC2
Number of Residues5
Detailsbinding site for residue NA A 702
ChainResidue
AILE582
AHOH1064
AASP440
AMET441
AASP581

site_idAC3
Number of Residues8
Detailsbinding site for residue NA A 703
ChainResidue
AALA93
AALA94
AARG148
ASER562
AHOH1206
BVAL79
BTHR80
BHOH804

site_idAC4
Number of Residues9
Detailsbinding site for residue EDO A 704
ChainResidue
ALEU42
AGLY43
AVAL44
APHE249
AASP250
AVAL251
AVAL327
AHOH897
AHOH1089

site_idAC5
Number of Residues7
Detailsbinding site for residue EDO A 705
ChainResidue
AILE39
AALA40
ALEU42
AVAL251
AGLN306
ASER329
AHOH1048

site_idAC6
Number of Residues6
Detailsbinding site for residue CU B 701
ChainResidue
BTYQ382
BHIS431
BHIS433
BHIS592
BHOH805
BHOH1284

site_idAC7
Number of Residues5
Detailsbinding site for residue NA B 702
ChainResidue
BASP440
BMET441
BASP581
BILE582
BHOH1092

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
ATYQ382
BTYQ382

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
ATYQ382
BTYQ382

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PDB entries from 2024-05-01

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