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

4GGH

Crystal structure of an enolase family member from vibrio harveyi (efi-target 501692) with homology to mannonate dehydratase, with mg, hepes, and ethylene glycol bound (ordered loops, space group c2221)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0009063biological_processamino acid catabolic process
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0009063biological_processamino acid catabolic process
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0009063biological_processamino acid catabolic process
C0046872molecular_functionmetal ion binding
D0000287molecular_functionmagnesium ion binding
D0009063biological_processamino acid catabolic process
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASN247
BASN247
CASN247
DASN247
DHOH501
DHOH502

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AHOH501
AHOH502
AHOH925
AASP205
AGLU231
AGLU257

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EPE A 403
ChainResidue
AARG18
AHIS19
AGLN41
AARG382
AHIS384
ATRP386
AHOH651
AHOH762
AHOH765
AHOH815

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 404
ChainResidue
AARG118
AASP119
CASP69
CHOH862
DTHR171
DGLY394

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 405
ChainResidue
APRO170
AGLN172
AGLY173
ATYR175

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 406
ChainResidue
AGLN224
AASN226
ASER250
AHOH677
DGLN221

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 407
ChainResidue
AGLN41
AGLN42
ATRP80
AHIS307
APRO309
AASP311
AHOH921

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 408
ChainResidue
APRO383
AHIS384
AGLU385
AHOH615

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 401
ChainResidue
BASP205
BGLU231
BGLU257
BHOH501
BHOH502
BHOH906

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE EPE B 402
ChainResidue
BARG18
BHIS19
BGLN41
BARG209
BARG382
BHIS384
BTRP386
BHOH725
BHOH734
BHOH803
BHOH809

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 403
ChainResidue
BASN226
BSER250
BHOH632
CGLN221

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 404
ChainResidue
BASP69
BTHR171
BARG390
BGLY394
BHOH692
DARG118
DASP119

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 405
ChainResidue
BGLN41
BGLN42
BTYR79
BTRP80
BHIS307
BPRO309
BASP311
BHOH802

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 406
ChainResidue
BLYS198
BPHE200

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 401
ChainResidue
CASP205
CGLU231
CGLU257
CHOH501
CHOH502
CHOH925

site_idBC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL C 402
ChainResidue
DTYR79
DTRP80
CGLN41
CGLN42
CHIS207
CGLU257
CHIS307
CPRO309
CASP311

site_idBC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EPE C 403
ChainResidue
CARG18
CHIS19
CGLN41
CARG209
CARG382
CHIS384
CTRP386
CHOH678
CHOH734
CHOH814

site_idBC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO C 404
ChainResidue
BPRO227
BPHE228
CASN213
CGLN214
CGLN217
CHOH552
CHOH579
CHOH788

site_idCC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO C 405
ChainResidue
BARG118
BASP119
CTHR171
CARG390
CGLY394
DASP69
DHOH655

site_idCC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO C 406
ChainResidue
AGLN221
CGLU223
CGLN224
CASN226
CSER250
CHOH849
CHOH863
CHOH875

site_idCC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO C 407
ChainResidue
CPRO161
CGLN172
CGLY173

site_idCC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CL C 408
ChainResidue
CASN82
CGLY83
CPRO84
CVAL85
CILE86
DASN82
DGLY83
DPRO84
DVAL85
DILE86

site_idCC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL C 409
ChainResidue
CPRO383
CHIS384
CGLU385
CHOH683

site_idCC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL C 410
ChainResidue
ALEU391
APRO392
AASP393
CHOH720

site_idCC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 401
ChainResidue
DASP205
DGLU231
DGLU257
DHOH503
DHOH504
DHOH928

site_idCC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL D 402
ChainResidue
CTRP80
DGLN41
DGLN42
DHIS207
DGLU257
DHIS307
DPRO309
DASP311

site_idCC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EPE D 403
ChainResidue
DARG18
DHIS19
DGLN41
DARG209
DARG382
DHIS384
DTRP386
DHOH623
DHOH657
DHOH857

site_idDC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO D 404
ChainResidue
BASN213
BGLN214
BGLN217
BHOH508
BHOH529
BHOH756
DPRO227

site_idDC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO D 405
ChainResidue
DPRO170
DTHR171
DGLN172
DGLY173
DTYR175

site_idDC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO D 406
ChainResidue
APRO227
APHE228
DASN213
DGLN214
DGLN217
DHOH620
DHOH680

Functional Information from PROSITE/UniProt
site_idPS00908
Number of Residues26
DetailsMR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AiSGVDmALwDIkAKianmPLhqLFG
ChainResidueDetails
AALA89-GLY114

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:24697546
ChainResidueDetails
AASP205
AGLU231
AGLU257
BASP205
BGLU231
BGLU257
CASP205
CGLU231
CGLU257
DASP205
DGLU231
DGLU257

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG278
AHIS307
AGLU334
BHIS207
BARG278
BHIS307
BGLU334
CHIS207
CARG278
CGLU334
DHIS207
DARG278
DHIS307
DGLU334
AHIS207
CHIS307

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon