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1M22

X-ray structure of native peptide amidase from Stenotrophomonas maltophilia at 1.4 A

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE EPE A 2001
ChainResidue
AARG248
AHOH2432
AHOH2601
APHE256
AASP285
APRO286
AALA287
ALEU417
AHOH2192
AHOH2199
AHOH2335

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EPE B 3001
ChainResidue
BARG248
BPHE256
BASP285
BPRO286
BALA287
BHOH3204
BHOH3211
BHOH3243
BHOH3441

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 726
ChainResidueDetails
ALYS123electrostatic stabiliser, proton acceptor, proton donor
ASER202electrostatic stabiliser, proton acceptor, proton donor, proton relay
ASER226nucleofuge, nucleophile, proton acceptor, proton donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 726
ChainResidueDetails
BLYS123electrostatic stabiliser, proton acceptor, proton donor
BSER202electrostatic stabiliser, proton acceptor, proton donor, proton relay
BSER226nucleofuge, nucleophile, proton acceptor, proton donor

246031

PDB entries from 2025-12-10

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