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8XJ4

Structure of prostatic acid phosphatase in human semen

Functional Information from PROSITE/UniProt
site_idPS00616
Number of Residues15
DetailsHIS_ACID_PHOSPHAT_1 Histidine acid phosphatases phosphohistidine signature. LkfVtlVfRHGdRsP
ChainResidueDetails
BLEU35-PRO49

site_idPS00778
Number of Residues17
DetailsHIS_ACID_PHOSPHAT_2 Histidine acid phosphatases active site signature. LiMYsAHDTTVsgLqmA
ChainResidueDetails
BLEU283-ALA299

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:1989985
ChainResidueDetails
BHIS44
AHIS44

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:1989985
ChainResidueDetails
BASP290
AASP290

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:9804805
ChainResidueDetails
BARG43
BARG47
BARG111
BHIS289
AARG43
AARG47
AARG111
AHIS289

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for substrate specificity
ChainResidueDetails
BPRO49
APRO49

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Required for homodimerization => ECO:0000250|UniProtKB:P20646
ChainResidueDetails
BTRP138
BHIS144
ATRP138
AHIS144

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Required for structural stability => ECO:0000269|PubMed:9584846
ChainResidueDetails
BTRP206
ATRP206

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10639192
ChainResidueDetails
BASN94
AASN94

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10639192, ECO:0000269|PubMed:12525165
ChainResidueDetails
BASN220
AASN220

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12525165
ChainResidueDetails
BASN333
AASN333

222624

PDB entries from 2024-07-17

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