Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2ALP

REFINED STRUCTURE OF ALPHA-LYTIC PROTEASE AT 1.7 ANGSTROMS RESOLUTION. ANALYSIS OF HYDROGEN BONDING AND SOLVENT STRUCTURE

Replaces:  1ALP
Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
AHIS57
AARG122
AARG192
AGLY193
ASER195
AHOH270
AHOH296
AHOH332

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 2
ChainResidue
AASN15
AARG230
APRO233
AHOH276
AHOH303
AHOH349
AHOH363
AALA15

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAGHC
ChainResidueDetails
AVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. CMgrGDSGGSWI
ChainResidueDetails
ACYS189-ILE200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1ssx
ChainResidueDetails
AASP102
ASER195
AGLY193
AHIS57
ASER214

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ssx
ChainResidueDetails
AASP102
ASER195
AGLY193
AHIS57

site_idMCSA1
Number of Residues5
DetailsM-CSA 609
ChainResidueDetails
AHIS57proton acceptor, proton donor
AASP102electrostatic stabiliser
AGLY193electrostatic stabiliser
ASER195electrostatic stabiliser
ASER214electrostatic stabiliser

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon