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4K90

Extracellular metalloproteinase from Aspergillus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0005615cellular_componentextracellular space
A0008270molecular_functionzinc ion binding
B0004222molecular_functionmetalloendopeptidase activity
B0005615cellular_componentextracellular space
B0008270molecular_functionzinc ion binding
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. IVIHEYTHGL
ChainResidueDetails
AILE426-LEU435

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:24100314, ECO:0007744|PDB:4K90
ChainResidueDetails
BGLU245

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:24100314, ECO:0007744|PDB:4K90
ChainResidueDetails
ALEU375
AASP378
AASP400
AASN437
AARG438
ATHR440
AGLY442
AASN445
AGLU459
BASN47

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:24100314, ECO:0007744|PDB:4K90
ChainResidueDetails
AHIS433
AHIS429

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Important for proper folding of the protein and catalytic activity => ECO:0000305|PubMed:24100314
ChainResidueDetails
AARG470

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN286

221051

PDB entries from 2024-06-12

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