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4ES7

crystal structure of protein HC from Homo sapiens at 2 angstrom

Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 201
ChainResidue
ALYS111
AGLY165
AGLN167
APEG202

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 202
ChainResidue
ATYR72
AMET92
ALYS123
APEG201
APEG203

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 203
ChainResidue
AMET55
ATYR72
ALYS123
ATYR125
APEG202

Functional Information from PROSITE/UniProt
site_idPS00213
Number of Residues14
DetailsLIPOCALIN Lipocalin signature. NFNisRIYGKWYNL
ChainResidueDetails
AASN8-LEU21

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBinding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"1714898","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"10631976","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"1694784","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"1694784","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22171320","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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