Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2R3B

CRYSTAL STRUCTURE OF a ribokinase-like superfamily protein (EF1790) FROM ENTEROCOCCUS FAECALIS V583 AT 1.80 A RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0046496biological_processnicotinamide nucleotide metabolic process
A0047453molecular_functionATP-dependent NAD(P)H-hydrate dehydratase activity
A0052855molecular_functionADP-dependent NAD(P)H-hydrate dehydratase activity
A0052856molecular_functionNADHX epimerase activity
A0052857molecular_functionNADPHX epimerase activity
A0110051biological_processmetabolite repair
B0005524molecular_functionATP binding
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
B0046496biological_processnicotinamide nucleotide metabolic process
B0047453molecular_functionATP-dependent NAD(P)H-hydrate dehydratase activity
B0052855molecular_functionADP-dependent NAD(P)H-hydrate dehydratase activity
B0052856molecular_functionNADHX epimerase activity
B0052857molecular_functionNADPHX epimerase activity
B0110051biological_processmetabolite repair
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 292
ChainResidue
BHOH373
BHOH419
BHOH420
BHOH431
BHOH462
BHOH512

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 292
ChainResidue
AHOH551
AHOH554
AHOH405
AHOH515
AHOH547

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 293
ChainResidue
AASN34
AARG35
AHOH340

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 293
ChainResidue
BGLY213
BGLY215
BASP216
BHOH522

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CL B 294
ChainResidue
AHIS69
AALA75
BTYR37
BGLY38
BGLY39
BALA40
BEDO296

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 295
ChainResidue
BTYR269
BLYS272

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 294
ChainResidue
AHIS153
ATHR211
AGLY213
ATHR214
AGLY215
AASP216
BLYS22

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 295
ChainResidue
ATYR269
ALYS272

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 296
ChainResidue
AGLU74
AMSE76
BALA40
BMSE43
BASP216
BCL294
BHOH372
BHOH522

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 297
ChainResidue
BGLN122
BLYS147
BHOH553

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 296
ChainResidue
AGLU146
AGLN177
AGLY181
ATHR183
AHIS195
AALA196
AILE233
AHOH558

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 298
ChainResidue
BSER136
BGLN137
BARG159
BHIS162
BHOH545
BHOH591

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 299
ChainResidue
BGLU146
BGLY181
BSER182
BTHR183
BHIS195
BALA196
BILE233
BEDO300

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 300
ChainResidue
BGLU146
BLYS147
BPRO231
BEDO299
BHOH583

Functional Information from PROSITE/UniProt
site_idPS01049
Number of Residues11
DetailsYJEF_C_1 YjeF C-terminal domain signature 1. VILIGPGLGlD
ChainResidueDetails
AVAL95-ASP105

site_idPS01050
Number of Residues11
DetailsYJEF_C_2 YjeF C-terminal domain signature 2. GGtGDTLAGiI
ChainResidueDetails
AGLY212-ILE222

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01965
ChainResidueDetails
AALA40
AGLY103
AASP216
BALA40
BGLY103
BHIS153
BGLY215
BASP216
AHIS153
AGLY215

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon