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3HOA

Crystal structure of the Thermus thermophilus M32 carboxypeptidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004180molecular_functioncarboxypeptidase activity
A0004181molecular_functionmetallocarboxypeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0004180molecular_functioncarboxypeptidase activity
B0004181molecular_functionmetallocarboxypeptidase activity
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL B 510
ChainResidue
BARG239
BLEU240

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. GTLHEMGHAL
ChainResidueDetails
AGLY273-LEU282

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1i1i
ChainResidueDetails
AGLU306
ATYR430

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1i1i
ChainResidueDetails
BGLU306
BTYR430

248335

PDB entries from 2026-01-28

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