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4OK2

Crystal Structure of Alg17c Mutant Y258A

Functional Information from GO Data
ChainGOidnamespacecontents
A0016829molecular_functionlyase activity
A0042597cellular_componentperiplasmic space
B0016829molecular_functionlyase activity
B0042597cellular_componentperiplasmic space
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 801
ChainResidue
AHIS415
AASP433
AHIS464
AHOH903
AHOH1139

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 801
ChainResidue
BHOH1079
BHIS415
BASP433
BHIS464
BHOH901

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:24478312
ChainResidueDetails
AALA258
BALA258

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:B2FSW8
ChainResidueDetails
AHIS413
BHIS413

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:24478312, ECO:0007744|PDB:4OJZ
ChainResidueDetails
ALYS136
BLYS198
BHIS202
BTYR257
BARG438
BGLU667
AGLN146
ALYS198
AHIS202
ATYR257
AARG438
AGLU667
BLYS136
BGLN146

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:24478312, ECO:0007744|PDB:4NEI, ECO:0007744|PDB:4OJZ, ECO:0007744|PDB:4OK2, ECO:0007744|PDB:4OK4
ChainResidueDetails
AHIS415
AASP433
AHIS464
BHIS415
BASP433
BHIS464

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Neutralizes the sugar carboxylate group at subsite +1 => ECO:0000305|PubMed:24478312
ChainResidueDetails
AASN201
AHIS202
BASN201
BHIS202

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PDB entries from 2024-09-11

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