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1SIH

AGAO in covalent complex with the inhibitor MOBA ("4-(4-methylphenoxy)-2-butyn-1-amine")

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
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 1101
ChainResidue
AASP316
ACYS317
ALEU318
AHIS345
AGLY350
AARG367
AHOH1245
AHOH1324
AHOH1646

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 701
ChainResidue
AHIS431
AHIS433
AHIS592
AHOH1368

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 703
ChainResidue
AASP440
AMET441
AASP581
AILE582
AHOH1208

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 1201
ChainResidue
AARG532
AARG533
ATHR554
APHE557
AHIS561
ASER562
AGLY563
AGLY564
AALA565
AHOH1214

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1202
ChainResidue
AASN126
AASP161
AVAL197
AALA199
AHOH1502

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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P12807
ChainResidueDetails
AASP298

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Schiff-base intermediate with substrate; via topaquinone => ECO:0000250|UniProtKB:P12807
ChainResidueDetails
AMBQ382

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P12807
ChainResidueDetails
ATYR296

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P46883
ChainResidueDetails
AILE379

site_idSWS_FT_FI5
Number of Residues3
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

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: 2',4',5'-topaquinone => ECO:0000269|PubMed:9405045
ChainResidueDetails
AMBQ382

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

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PDB entries from 2024-07-24

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