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6F75

Carboxypeptidase T mutant L254N with Sulphamoil Leucine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004181molecular_functionmetallocarboxypeptidase activity
A0006508biological_processproteolysis
A0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 401
ChainResidue
AHIS69
AGLU72
AHIS204
ALU0407

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 402
ChainResidue
AHOH756
ASER7
ATYR9
AGLU14
AHOH620
AHOH693

site_idAC3
Number of Residues5
Detailsbinding site for residue CA A 403
ChainResidue
ASER50
AASP51
AGLU57
AGLU59
AHOH565

site_idAC4
Number of Residues4
Detailsbinding site for residue CA A 404
ChainResidue
ATYR5
AASP291
AHOH702
AHOH703

site_idAC5
Number of Residues6
Detailsbinding site for residue CA A 405
ChainResidue
AASP56
AGLU57
AGLU61
AGLU104
AHOH517
AHOH676

site_idAC6
Number of Residues8
Detailsbinding site for residue SO4 A 406
ChainResidue
APHE174
AARG183
AASN187
ATRP264
AGLN268
AHOH512
AHOH513
AHOH548

site_idAC7
Number of Residues11
Detailsbinding site for residue LU0 A 407
ChainResidue
AHIS69
AGLU72
AARG129
AASN146
AARG147
AHIS204
ATHR205
ATYR255
AGLU277
AZN401
AHOH636

site_idAC8
Number of Residues7
Detailsbinding site for residue SO4 A 408
ChainResidue
ASER138
ASER139
ATYR140
AARG171
ASER172
AHOH515
AHOH584

Functional Information from PROSITE/UniProt
site_idPS00132
Number of Residues23
DetailsCARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PeVlYtaLhHArEhLTVemalyT
ChainResidueDetails
APRO60-THR82

site_idPS00133
Number of Residues11
DetailsCARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HTYSELIlYPY
ChainResidueDetails
AHIS204-TYR214

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000305|PubMed:1521526
ChainResidueDetails
AGLU277

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:1521526
ChainResidueDetails
AHIS69
AGLU72
AHIS204

237992

PDB entries from 2025-06-25

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