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2OF9

Crystal structure of apo AVR4 (D39A/C122S)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0009374molecular_functionbiotin binding
B0005576cellular_componentextracellular region
B0009374molecular_functionbiotin binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 402
ChainResidue
ASER71
AHOH429
AHOH503

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 403
ChainResidue
ATRP68
ATHR75
AHOH426
AHOH429

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 405
ChainResidue
AARG56
BHOH63
BHOH73
BHIS267
AHIS54
ALYS55

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 406
ChainResidue
ASER105
ATYR106
BFMT413

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 409
ChainResidue
AVAL101
AASN102
ATYR106

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 412
ChainResidue
ALYS88
ATHR119
AARG120
AHOH430
BLYS209

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 415
ChainResidue
AGLU28
AARG85
BTHR230

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT B 401
ChainResidue
BHOH58
BHOH62
BHOH81
BALA238
BSER271

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT B 404
ChainResidue
BHOH31
BHOH58
BTRP268
BTHR275

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT B 407
ChainResidue
AGLN59
APHE82
AILE83
BHOH101
BASP303
BILE304

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT B 408
ChainResidue
AHIS67
AHOH456
AHOH459
BHIS254
BLYS255
BARG256

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT B 410
ChainResidue
AALA36
BTHR232
BLEU246
BPRO248

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT B 411
ChainResidue
AASP103
AILE104
BGLN259
BPHE282
BILE283

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT B 413
ChainResidue
ASER105
ATYR106
ATRP108
AFMT406
BHOH60
BHOH77
BVAL237

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT B 414
ChainResidue
BHOH157
BVAL301
BASN302
BTYR306
BLYS309

Functional Information from PROSITE/UniProt
site_idPS00577
Number of Residues15
DetailsAVIDIN_1 Avidin-like domain signature. YdwKAtrVGyNnFTR
ChainResidueDetails
ATYR106-ARG120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15858262","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Y52","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y55","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15858262","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Y52","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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