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1LOK

The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris: A Tale of Buffer Inhibition

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008235molecular_functionmetalloexopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 901
ChainResidue
AASP117
AGLU152
AHIS256
ATRS800
AZN902

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN A 902
ChainResidue
AASP179
ATRS800
AZN901
AHIS97
AASP117
AGLU151
AGLU152

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 903
ChainResidue
ATYR218
AHOH1024
AHOH1035
AHOH1043
AHOH1045
AHOH1095

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SCN A 1973
ChainResidue
AASN171
AVAL172
ATYR238
APRO239
AHOH1192

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE TRS A 800
ChainResidue
AHIS97
AASP117
AGLU151
AGLU152
AASP179
AMET180
ATYR225
ACYS227
AHIS256
AZN901
AZN902
AHOH1116
AHOH1293

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 167
ChainResidueDetails
AHIS97metal ligand
AASP117metal ligand
AGLU151hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLU152metal ligand
AASP179metal ligand
AHIS256metal ligand

218853

PDB entries from 2024-04-24

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