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4FXY

Crystal structure of rat neurolysin with bound pyrazolidin inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
P0004222molecular_functionmetalloendopeptidase activity
P0005737cellular_componentcytoplasm
P0005739cellular_componentmitochondrion
P0005758cellular_componentmitochondrial intermembrane space
P0005829cellular_componentcytosol
P0005886cellular_componentplasma membrane
P0006111biological_processregulation of gluconeogenesis
P0006508biological_processproteolysis
P0006518biological_processpeptide metabolic process
P0008233molecular_functionpeptidase activity
P0008237molecular_functionmetallopeptidase activity
P0030163biological_processprotein catabolic process
P0042277molecular_functionpeptide binding
P0043171biological_processpeptide catabolic process
P0046872molecular_functionmetal ion binding
P0070012molecular_functionoligopeptidase activity
P1902809biological_processregulation of skeletal muscle fiber differentiation
Q0004222molecular_functionmetalloendopeptidase activity
Q0005737cellular_componentcytoplasm
Q0005739cellular_componentmitochondrion
Q0005758cellular_componentmitochondrial intermembrane space
Q0005829cellular_componentcytosol
Q0005886cellular_componentplasma membrane
Q0006111biological_processregulation of gluconeogenesis
Q0006508biological_processproteolysis
Q0006518biological_processpeptide metabolic process
Q0008233molecular_functionpeptidase activity
Q0008237molecular_functionmetallopeptidase activity
Q0030163biological_processprotein catabolic process
Q0042277molecular_functionpeptide binding
Q0043171biological_processpeptide catabolic process
Q0046872molecular_functionmetal ion binding
Q0070012molecular_functionoligopeptidase activity
Q1902809biological_processregulation of skeletal muscle fiber differentiation
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 0W2 P 701
ChainResidue
PTHR45
PILE123
PSER146
PARG491
PHOH837
PHOH838
PHOH927
PTYR49
PLEU69
PILE72
PGLU73
PTYR76
PARG80
PASP110
PMET113

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN P 702
ChainResidue
PHIS474
PGLU475
PHIS478
PGLU503
PHOH843

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 0W2 Q 701
ChainResidue
QTHR45
QTYR49
QLEU69
QILE72
QGLU73
QTYR76
QARG80
QASP110
QMET113
QARG116
QILE123
QSER146
QARG491
QHOH928
QHOH929
QHOH930

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN Q 702
ChainResidue
QHIS474
QGLU475
QHIS478
QGLU503
QHOH836

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TYFHEFGHVM
ChainResidueDetails
PTHR471-MET480

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095
ChainResidueDetails
PGLU475
QGLU475

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10095
ChainResidueDetails
PHIS474
PHIS478
PHIS481
QHIS474
QHIS478
QHIS481

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9BYT8
ChainResidueDetails
PLYS641
QLYS641

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 638
ChainResidueDetails
PHIS474
PGLU475
PHIS478
PGLU503proton shuttle (general acid/base)
PTYR613electrostatic stabiliser

site_idMCSA2
Number of Residues5
DetailsM-CSA 638
ChainResidueDetails
QHIS474
QGLU475
QHIS478
QGLU503proton shuttle (general acid/base)
QTYR613electrostatic stabiliser

223790

PDB entries from 2024-08-14

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