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1J9M

K38H mutant of Streptomyces K15 DD-transpeptidase

Replaces:  1EQS
Functional Information from GO Data
ChainGOidnamespacecontents
A0004180molecular_functioncarboxypeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008360biological_processregulation of cell shape
A0009002molecular_functionserine-type D-Ala-D-Ala carboxypeptidase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 600
ChainResidue
ASER35
ASER96
ALYS213
ATHR214
AGLY215
ACL601

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 601
ChainResidue
AARG248
ANA600
ALYS186
AGLY215
ASER216

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000269|PubMed:2764892
ChainResidueDetails
ASER35

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:2764892
ChainResidueDetails
AHIS38

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:2764892
ChainResidueDetails
ASER96

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ALYS213

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PDB entries from 2024-07-24

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