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4PZ4

High-resolution crystal structure of the human CD44 hyaluronan binding domain in new space group

Functional Information from GO Data
ChainGOidnamespacecontents
A0005540molecular_functionhyaluronic acid binding
A0007155biological_processcell adhesion
A0016020cellular_componentmembrane
B0005540molecular_functionhyaluronic acid binding
B0007155biological_processcell adhesion
B0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 201
ChainResidue
AARG41
ATYR42
AARG78
APEG204
AHOH307
AHOH310
BCYS77
BARG78
BPEG203

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 202
ChainResidue
AARG29
APHE34
APHE56
AASN120
AVAL132

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 203
ChainResidue
AALA31
AASN120
AALA123
APRO125

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG A 204
ChainResidue
ATYR42
ATHR111
AGLN113
ATYR114
ASO4201
AHOH407
BASN94

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 205
ChainResidue
ATHR62
AALA64
AGLN65
AHOH357
AHOH382
AHOH390
AHOH399
BASP140
BGLY141

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 206
ChainResidue
ATHR27
ACYS28
AHOH375
AHOH394
AHOH411

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 207
ChainResidue
AASN94
AILE96
BSO4201
BHOH355

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG A 208
ChainResidue
AASP23
AASN25
AASN39
AGLY40
BASP23
BASN25
BGLY40

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 201
ChainResidue
ACYS77
AEDO207
BARG41
BTYR42
BARG78
BPEG203
BHOH315
BHOH325

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 202
ChainResidue
BARG46
BGLU83
BGLY84
BPEG208
BPEG208
BHOH349
BHOH380

site_idBC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PEG B 203
ChainResidue
AGLU37
AGLY40
AARG41
AARG78
ASO4201
BGLU37
BGLY40
BARG41
BARG78
BSO4201
BHOH368

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 204
ChainResidue
BARG29
BPHE56
BSER58
BASN120
BVAL132

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 205
ChainResidue
BALA138
BPHE139
BGLN157
BLYS158

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 206
ChainResidue
BALA20
BILE143
BARG162
BHOH322
BHOH323

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS B 207
ChainResidue
ASER95
AILE96
BTYR79
BHOH372

site_idBC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PEG B 208
ChainResidue
BSO4202
BSO4202
BHOH304
BHOH380
BHOH380
BARG46
BHIS85
BVAL86
BSER109
BSER109

Functional Information from PROSITE/UniProt
site_idPS01241
Number of Residues45
DetailsLINK_1 Link domain signature. CkafnstlptmaqmekAlsi.GfetCryGfieghvvi.PrihpnsiC
ChainResidueDetails
ACYS53-CYS97

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues176
DetailsDomain: {"description":"Link","evidences":[{"source":"PROSITE-ProRule","id":"PRU00323","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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