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5QIC

PanDDA analysis group deposition of models with modelled events (e.g. bound ligands) -- Crystal Structure of HAO1 in complex with Z30620520

Functional Information from GO Data
ChainGOidnamespacecontents
A0001561biological_processfatty acid alpha-oxidation
A0003973molecular_function(S)-2-hydroxy-acid oxidase activity
A0005777cellular_componentperoxisome
A0005782cellular_componentperoxisomal matrix
A0005829cellular_componentcytosol
A0006545biological_processglycine biosynthetic process
A0006979biological_processresponse to oxidative stress
A0008652biological_processamino acid biosynthetic process
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0043231cellular_componentintracellular membrane-bounded organelle
A0046296biological_processglycolate catabolic process
A0047969molecular_functionglyoxylate oxidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue FMN A 401
ChainResidue
ATYR26
ALYS236
ASER258
AHIS260
AGLY261
AARG263
AASP291
AGLY292
AGLY293
AARG295
AGLY314
ATYR27
AARG315
AHOH513
AHOH571
AHOH596
AALA79
ATHR80
AALA81
ASER108
AGLN130
ATYR132
ATHR158

site_idAC2
Number of Residues12
Detailsbinding site for residue GX4 A 402
ChainResidue
ATYR134
ALYS135
AASP136
AVAL139
AMET183
APHE186
ATYR208
ATYR208
AVAL209
ALYS211
AALA212
AHOH612

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
ASER258-GLN264

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00683
ChainResidueDetails
AHIS260

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18215067, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDU
ChainResidueDetails
ATYR26
ATYR132
AHIS260
AARG263

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U
ChainResidueDetails
AALA79

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00683, ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U
ChainResidueDetails
ASER108
ATHR158
ALYS236

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00683, ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2W0U
ChainResidueDetails
AGLN130

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18215067, ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDU
ChainResidueDetails
AARG167

site_idSWS_FT_FI7
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U
ChainResidueDetails
ASER258
AASP291
AGLY314

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9WU19
ChainResidueDetails
ALYS184

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9WU19
ChainResidueDetails
ASER194

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER230

229380

PDB entries from 2024-12-25

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