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5AO5

Endo180 D1-4, monoclinic form

Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 901
ChainResidue
AGLN326
AASP328
AGLU333
AASN348
AHOH2078

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 902
ChainResidue
AHOH2092
AGLU470
AASN472
AASP493
AHOH2090

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 901
ChainResidue
BGLN326
BASP328
BGLU333
BASN348
BHOH2053

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 902
ChainResidue
BGLU470
BASN472
BASP493
BHOH2066
BHOH2067

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 1512
ChainResidue
ATHR216
AGLN217

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 1511
ChainResidue
BARG260
BASP350
BCYS351
BARG401
BHOH2052

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1513
ChainResidue
AGLY205
AARG206
ATYR219

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1512
ChainResidue
BARG206
BTRP212
BTYR219
BTRP225

Functional Information from PROSITE/UniProt
site_idPS00023
Number of Residues42
DetailsFN2_1 Fibronectin type-II collagen-binding domain signature. CtiPFkYdnqwfhgCtstgredghlWCattqDYgkderWgFC
ChainResidueDetails
ACYS187-CYS228

site_idPS00615
Number of Residues25
DetailsC_TYPE_LECTIN_1 C-type lectin domain signature. CGvirtessgg...WQNRDCsialp.YVC
ChainResidueDetails
ACYS335-CYS359
ACYS481-CYS504

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN69
BASN69

site_idSWS_FT_FI2
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN140
AASN364
BASN140
BASN364

223790

PDB entries from 2024-08-14

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