Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6A9V

Crystal structure of Icp55 from Saccharomyces cerevisiae (N-terminal 42 residues deletion)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0005634cellular_componentnucleus
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0016020cellular_componentmembrane
A0016485biological_processprotein processing
A0016787molecular_functionhydrolase activity
A0030145molecular_functionmanganese ion binding
A0046872molecular_functionmetal ion binding
A0050821biological_processprotein stabilization
A0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MN A 601
ChainResidue
AASP327
AASP338
ASER340
AGLU467
AMN602
AGLY604

site_idAC2
Number of Residues6
Detailsbinding site for residue MN A 602
ChainResidue
AGLU467
AMN601
AGLY604
AASP338
AHIS417
AGLU444

site_idAC3
Number of Residues2
Detailsbinding site for residue PGE A 603
ChainResidue
AILE309
AGLU444

site_idAC4
Number of Residues9
Detailsbinding site for residue GLY A 604
ChainResidue
ATYR296
AASP327
AASP338
AHIS417
AHIS424
AGLU444
AGLU467
AMN601
AMN602

Functional Information from PROSITE/UniProt
site_idPS00491
Number of Residues13
DetailsPROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HYIGHnLGLdVHD
ChainResidueDetails
AHIS413-ASP425

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AASP327
AASP338
AHIS417
AGLU444
AGLU467

218196

PDB entries from 2024-04-10

PDB statisticsPDBj update infoContact PDBjnumon