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6HF6

Crystal structure of the Protease 1 (E29A,E60A,E80A) from Pyrococcus horikoshii co-crystallized with Tb-Xo4.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0036524molecular_functionprotein deglycase activity
B0005737cellular_componentcytoplasm
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0036524molecular_functionprotein deglycase activity
C0005737cellular_componentcytoplasm
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0036524molecular_functionprotein deglycase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue 7MT A 201
ChainResidue
AALA8
AASN9
APHE35
AGLU36
AARG75
AMLI202

site_idAC2
Number of Residues3
Detailsbinding site for residue MLI A 202
ChainResidue
AASN9
AARG75
A7MT201

site_idAC3
Number of Residues2
Detailsbinding site for residue TB A 204
ChainResidue
AGLU10
AHOH456

site_idAC4
Number of Residues7
Detailsbinding site for residue 7MT B 201
ChainResidue
BALA8
BASN9
BPHE35
BGLU36
BARG75
BMLI202
BHOH386

site_idAC5
Number of Residues4
Detailsbinding site for residue MLI B 202
ChainResidue
BASN9
BARG75
B7MT201
BHOH386

site_idAC6
Number of Residues2
Detailsbinding site for residue TB B 203
ChainResidue
BHOH397
BHOH450

site_idAC7
Number of Residues6
Detailsbinding site for residue 7MT C 201
ChainResidue
CALA8
CASN9
CPHE35
CGLU36
CARG75
CMLI202

site_idAC8
Number of Residues3
Detailsbinding site for residue MLI C 202
ChainResidue
CASN9
CARG75
C7MT201

site_idAC9
Number of Residues3
Detailsbinding site for residue TB C 203
ChainResidue
BHOH417
CHOH364
CHOH373

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:11114201
ChainResidueDetails
ACYS100
BCYS100
CCYS100

site_idSWS_FT_FI2
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00608
ChainResidueDetails
AHIS101
BHIS101
CHIS101

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 964
ChainResidueDetails
AGLY70electrostatic stabiliser
AARG71electrostatic stabiliser
AGLU74electrostatic stabiliser, modifies pKa
ACYS100covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
AHIS101electrostatic stabiliser, proton acceptor, proton donor
ATYR120electrostatic stabiliser

site_idMCSA2
Number of Residues6
DetailsM-CSA 964
ChainResidueDetails
BGLY70electrostatic stabiliser
BARG71electrostatic stabiliser
BGLU74electrostatic stabiliser, modifies pKa
BCYS100covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
BHIS101electrostatic stabiliser, proton acceptor, proton donor
BTYR120electrostatic stabiliser

site_idMCSA3
Number of Residues6
DetailsM-CSA 964
ChainResidueDetails
CGLY70electrostatic stabiliser
CARG71electrostatic stabiliser
CGLU74electrostatic stabiliser, modifies pKa
CCYS100covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
CHIS101electrostatic stabiliser, proton acceptor, proton donor
CTYR120electrostatic stabiliser

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PDB entries from 2024-07-24

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