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1AL7

THREE-DIMENSIONAL STRUCTURES OF GLYCOLATE OXIDASE WITH BOUND ACTIVE-SITE INHIBITORS

Functional Information from GO Data
ChainGOidnamespacecontents
A0003973molecular_function(S)-2-hydroxy-acid oxidase activity
A0005777cellular_componentperoxisome
A0009853biological_processphotorespiration
A0009854biological_processoxidative photosynthetic carbon pathway
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0051707biological_processresponse to other organism
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE FMN A 360
ChainResidue
ATYR24
ALYS230
ASER252
AHIS254
AARG257
AASP285
AGLY286
AGLY287
AARG289
AGLY308
AARG309
ATYR25
AHST361
AHOH363
AHOH398
AALA76
APRO77
ATHR78
AALA79
ASER106
AGLN127
ATHR155

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HST A 361
ChainResidue
ATYR24
ATRP108
ATYR129
ATYR131
ALEU161
AARG164
APHE172
AILE207
AHIS254
AARG257
AFMN360
AHOH659

Functional Information from PROSITE/UniProt
site_idPS00557
Number of Residues7
DetailsFMN_HYDROXY_ACID_DH_1 FMN-dependent alpha-hydroxy acid dehydrogenases active site. SNHGARQ
ChainResidueDetails
ASER252-GLN258

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00683, ECO:0000305|PubMed:2644287
ChainResidueDetails
AHIS254

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9UJM8
ChainResidueDetails
ATYR24
ATYR129
AARG164
AHIS254
AARG257

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:2681790, ECO:0000269|PubMed:9144771, ECO:0007744|PDB:1AL7, ECO:0007744|PDB:1GOX
ChainResidueDetails
APRO77
AGLN127
ATHR155
ALYS230
ASER252
AASP285
AGLY308

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:9144771, ECO:0007744|PDB:1AL7
ChainResidueDetails
ASER106

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Involved in determining the substrate specificity of glycolate oxidase => ECO:0000305|PubMed:7705356
ChainResidueDetails
ATRP108

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|PubMed:3286256
ChainResidueDetails
AMET1

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1fcb
ChainResidueDetails
ATYR24
AHIS254
AARG257
ATYR129
AASP157

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1fcb
ChainResidueDetails
AHIS254
AARG257
ATYR129
AASP157

site_idMCSA1
Number of Residues5
DetailsM-CSA 852
ChainResidueDetails
ASER106electrostatic stabiliser
ATYR129electrostatic stabiliser, modifies pKa
ATHR155electrostatic stabiliser
ALYS230electrostatic stabiliser, enhance reactivity
AHIS254proton shuttle (general acid/base)

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PDB entries from 2024-07-10

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