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2WQ8

Glycan labelling using engineered variants of galactose oxidase obtained by directed evolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0016491molecular_functionoxidoreductase activity
A0045480molecular_functiongalactose oxidase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CU A 1640
ChainResidue
APHE227
ACYS228
ATYR272
ATYR495
AHIS496
AHIS581
AACY1642

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1641
ChainResidue
AASN34
ATHR37
AALA141
AGLU142
ALYS29
AASP32

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY A 1642
ChainResidue
ATYR272
APHE290
ATYR495
AHIS496
ACU1640

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ACY A 1643
ChainResidue
AARG371
AALA378
AALA381
ATHR398
AGLY400
AASN413
AALA414
AHIS415
AEDO1644

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 1644
ChainResidue
AALA378
APRO379
AALA381
AGLY400
AGLY401
ATHR411
AASN413
AACY1643
AHOH2375

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 1645
ChainResidue
AASN385
AALA386
AVAL387
ATHR443
ASER444
ATHR582
AGLN587
AEDO1646
AHOH2333

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE EDO A 1646
ChainResidue
ATHR443
ASER497
AILE498
ASER499
AALA579
ATHR580
AHIS581
ATHR582
AVAL583
AEDO1645
AHOH2376

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 1647
ChainResidue
AILE475
AGLN486
APHE528
APRO530
AASN531
ATYR532
AGOL1655
AHOH2377

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 1648
ChainResidue
APRO72
ATRP81
AILE82
ATRP105
APHE106
AASP108
ALYS112
AALA132
AHOH2378

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 1649
ChainResidue
AHIS334
AALA335
ATRP336
AGLY384
ATHR582
AVAL583
AHOH2379
AHOH2380

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1650
ChainResidue
ALEU158
AASN314
ATYR436
ATYR484
ALYS485

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1651
ChainResidue
APRO156
AGLY157
ALEU158
AGLY159
AARG160
AASN531
AGLY538

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1652
ChainResidue
APRO591
ALEU592
ATHR593
AGLN605
APRO607

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1653
ChainResidue
APHE295
AGLU296
AASN298
AGLY299
ASER311
AVAL268

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1654
ChainResidue
AHIS40
AARG73
AASN79
AHOH2015
AHOH2381

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1655
ChainResidue
ATYR484
AGLN486
AASN531
AEDO1647
AHOH2382

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DGNQNGWIGrhEV
ChainResidueDetails
AASP75-VAL87

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|DOI:10.1007/s007750050139
ChainResidueDetails
ATYR495

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
ATYR272
ATYR495
AHIS496
AHIS581

site_idSWS_FT_FI3
Number of Residues2
DetailsCROSSLNK: 3'-(S-cysteinyl)-tyrosine (Cys-Tyr)
ChainResidueDetails
ACYS228
ATYR272

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 322
ChainResidueDetails
ACYS228activator, covalently attached, metal ligand
ATYR272activator, hydrogen radical acceptor, hydrogen radical donor, metal ligand
APHE290activator, radical stabiliser
ATYR495activator, metal ligand, proton acceptor, proton donor
AHIS496metal ligand
AHIS581metal ligand

222415

PDB entries from 2024-07-10

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