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2X8T

Crystal Structure of the Abn2 H318A mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1471
ChainResidue
AARG348
AARG366
AHOH2147
AHOH2219

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 1472
ChainResidue
AHOH2083
AGLY121
ASER123
AASN168
ATYR189
AHOH2081

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 473
ChainResidue
AHOH2008
AHOH2011
AHOH2074
AHOH2075
AHOH2106
AHOH2107
AHOH2149

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1473
ChainResidue
ATYR323
AGLU325
AHOH2152
AHOH2224
AHOH2225

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TRS B 1472
ChainResidue
BHIS37
BASP38
BTRP100
BASP171
BGLU224
BLEU246
BHOH2010
BHOH2259
BHOH2260
BHOH2261

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 1473
ChainResidue
BTYR313
BARG348
BHOH2172

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 474
ChainResidue
BHOH2009
BHOH2012
BHOH2089
BHOH2090
BHOH2127
BHOH2128
BHOH2175

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 1474
ChainResidue
BTYR323
BGLU325
BHOH2131
BHOH2176

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA B 476
ChainResidue
BHOH2172
BHOH2173

site_idBC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GOL B 1475
ChainResidue
BVAL104
BTHR105
BHIS173
BTHR174
BTYR227
BHOH2013
BHOH2059
BHOH2092
BHOH2129
BHOH2262
BHOH2263
BHOH2264

Functional Information from PROSITE/UniProt
site_idPS00867
Number of Residues8
DetailsCPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. ILEMNPKT
ChainResidueDetails
AILE195-THR202

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"20883454","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"20883454","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20883454","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20883454","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsSite: {"description":"Important for catalytic activity, responsible for pKa modulation of the active site Glu and correct orientation of both the proton donor and substrate","evidences":[{"source":"PubMed","id":"20883454","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsSite: {"description":"Important for substrate recognition"}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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