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4NV4

1.8 Angstrom Crystal Structure of Signal Peptidase I from Bacillus anthracis.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006465biological_processsignal peptide processing
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0016020cellular_componentmembrane
B0004252molecular_functionserine-type endopeptidase activity
B0006465biological_processsignal peptide processing
B0006508biological_processproteolysis
B0008236molecular_functionserine-type peptidase activity
B0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PG4 A 201
ChainResidue
ALYS75
AARG149
ALEU150
AGLY151
ASER152
AARG156
AHIS157
AHOH334
AHOH394

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG A 202
ChainResidue
ATYR99
AHOH417

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 203
ChainResidue
AASP106
AHOH400

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PG4 B 201
ChainResidue
BARG149
BLEU150
BSER152
BTRP153
BARG156
BHIS157
BPEG203
BHOH368
BHOH379

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PG4 B 202
ChainResidue
BTYR79
BPHE158
BHOH347

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG B 203
ChainResidue
BASP125
BGLU130
BLEU131
BPG4201

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 204
ChainResidue
BGLY88
BHIS90
BASN101
BLYS135

Functional Information from PROSITE/UniProt
site_idPS00501
Number of Residues8
DetailsSPASE_I_1 Signal peptidases I serine active site. GKSMMPTL
ChainResidueDetails
AGLY38-LEU45

site_idPS00760
Number of Residues13
DetailsSPASE_I_2 Signal peptidases I lysine active site. KRIIGlPGDhIeY
ChainResidueDetails
ALYS81-TYR93

site_idPS00761
Number of Residues14
DetailsSPASE_I_3 Signal peptidases I signature 3. IFVVGDNRlgSwdS
ChainResidueDetails
AILE142-SER155

246031

PDB entries from 2025-12-10

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