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1OVA

CRYSTAL STRUCTURE OF UNCLEAVED OVALBUMIN AT 1.95 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005615cellular_componentextracellular space
B0004867molecular_functionserine-type endopeptidase inhibitor activity
B0005615cellular_componentextracellular space
C0004867molecular_functionserine-type endopeptidase inhibitor activity
C0005615cellular_componentextracellular space
D0004867molecular_functionserine-type endopeptidase inhibitor activity
D0005615cellular_componentextracellular space
Functional Information from PROSITE/UniProt
site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. FRADHPFLFcI
ChainResidueDetails
APHE364-ILE374
CPHE364-ILE374
BPHE364-ILE374

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING:
ChainResidueDetails
CASP202
DASP202

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by elastase or subtilisin => ECO:0000269|PubMed:11931671
ChainResidueDetails
CSER359
DSER359

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Cleavage; by subtilisin => ECO:0000269|PubMed:11931671
ChainResidueDetails
CARG365
DARG365

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylglycine => ECO:0000269|PubMed:272676, ECO:0000269|PubMed:751625
ChainResidueDetails
CSER25
DSER25

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:6783411
ChainResidueDetails
CILE87
CALA351
DILE87
DALA351

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19358553, ECO:0000269|PubMed:1942038
ChainResidueDetails
CLEU299
DLEU299

224931

PDB entries from 2024-09-11

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