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5VFB

1.36 Angstrom Resolution Crystal Structure of Malate Synthase G from Pseudomonas aeruginosa in Complex with Glycolic Acid.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004474molecular_functionmalate synthase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006097biological_processglyoxylate cycle
A0006099biological_processtricarboxylic acid cycle
A0009436biological_processglyoxylate catabolic process
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0004474molecular_functionmalate synthase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006097biological_processglyoxylate cycle
B0006099biological_processtricarboxylic acid cycle
B0009436biological_processglyoxylate catabolic process
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue NI A 801
ChainResidue
AGLU432
AASP460
AGOA807
AHOH976
AHOH1054

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 802
ChainResidue
ALYS14
AVAL15
AHOH1415

site_idAC3
Number of Residues4
Detailsbinding site for residue CL A 803
ChainResidue
ATRP587
AHOH940
AHOH1934
AARG477

site_idAC4
Number of Residues4
Detailsbinding site for residue CL A 804
ChainResidue
APRO317
AASP318
AARG334
AHOH1530

site_idAC5
Number of Residues4
Detailsbinding site for residue CL A 805
ChainResidue
AARG57
AASN705
ATYR707
AHOH1285

site_idAC6
Number of Residues1
Detailsbinding site for residue CL A 806
ChainResidue
ALYS511

site_idAC7
Number of Residues12
Detailsbinding site for residue GOA A 807
ChainResidue
AARG340
AGLU432
AGLY457
APHE458
ALEU459
AASP460
ATRP539
ANI801
AHOH976
AHOH1054
AHOH1320
AHOH1447

site_idAC8
Number of Residues5
Detailsbinding site for residue NI B 801
ChainResidue
BGLU432
BASP460
BGOA809
BHOH954
BHOH1093

site_idAC9
Number of Residues6
Detailsbinding site for residue NA B 802
ChainResidue
AHOH1214
AHOH1237
AHOH1890
AHOH2010
BHOH1063
BHOH1447

site_idAD1
Number of Residues6
Detailsbinding site for residue NA B 803
ChainResidue
AHOH2007
BHOH931
BHOH1537
BHOH1745
BHOH1970
BHOH1972

site_idAD2
Number of Residues5
Detailsbinding site for residue CL B 804
ChainResidue
BGLU3
BLYS14
BVAL15
BHOH1140
BHOH1827

site_idAD3
Number of Residues3
Detailsbinding site for residue CL B 805
ChainResidue
BARG477
BTRP587
BHOH1907

site_idAD4
Number of Residues3
Detailsbinding site for residue CL B 806
ChainResidue
BHIS235
BASN236
BHOH1770

site_idAD5
Number of Residues2
Detailsbinding site for residue CL B 807
ChainResidue
BLYS511
BHOH1865

site_idAD6
Number of Residues13
Detailsbinding site for residue GOA B 809
ChainResidue
BARG340
BGLU432
BGLY457
BPHE458
BLEU459
BASP460
BTRP539
BALA633
BNI801
BHOH920
BHOH954
BHOH967
BHOH1093

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00641
ChainResidueDetails
AARG340
BARG340

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00641
ChainResidueDetails
AASP631
BASP631

site_idSWS_FT_FI3
Number of Residues18
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00641
ChainResidueDetails
AVAL118
BVAL118
BARG125
BSER276
BARG313
BARG340
BGLU432
BGLY457
BASP460
BPRO541
AARG125
ASER276
AARG313
AARG340
AGLU432
AGLY457
AASP460
APRO541

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000255|HAMAP-Rule:MF_00641
ChainResidueDetails
ACYS617
BCYS617

226707

PDB entries from 2024-10-30

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