Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1GK2

Histidine Ammonia-Lyase (HAL) Mutant F329G from Pseudomonas putida

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004397molecular_functionhistidine ammonia-lyase activity
A0005737cellular_componentcytoplasm
A0006547biological_processL-histidine metabolic process
A0006548biological_processL-histidine catabolic process
A0016829molecular_functionlyase activity
A0016841molecular_functionammonia-lyase activity
A0019556biological_processL-histidine catabolic process to glutamate and formamide
A0019557biological_processL-histidine catabolic process to glutamate and formate
B0003824molecular_functioncatalytic activity
B0004397molecular_functionhistidine ammonia-lyase activity
B0005737cellular_componentcytoplasm
B0006547biological_processL-histidine metabolic process
B0006548biological_processL-histidine catabolic process
B0016829molecular_functionlyase activity
B0016841molecular_functionammonia-lyase activity
B0019556biological_processL-histidine catabolic process to glutamate and formamide
B0019557biological_processL-histidine catabolic process to glutamate and formate
C0003824molecular_functioncatalytic activity
C0004397molecular_functionhistidine ammonia-lyase activity
C0005737cellular_componentcytoplasm
C0006547biological_processL-histidine metabolic process
C0006548biological_processL-histidine catabolic process
C0016829molecular_functionlyase activity
C0016841molecular_functionammonia-lyase activity
C0019556biological_processL-histidine catabolic process to glutamate and formamide
C0019557biological_processL-histidine catabolic process to glutamate and formate
D0003824molecular_functioncatalytic activity
D0004397molecular_functionhistidine ammonia-lyase activity
D0005737cellular_componentcytoplasm
D0006547biological_processL-histidine metabolic process
D0006548biological_processL-histidine catabolic process
D0016829molecular_functionlyase activity
D0016841molecular_functionammonia-lyase activity
D0019556biological_processL-histidine catabolic process to glutamate and formamide
D0019557biological_processL-histidine catabolic process to glutamate and formate
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1511
ChainResidue
ATYR53
ASER143
AASN313
ASER325
DTYR280
DARG283

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 1511
ChainResidue
CTYR280
CARG283
BTYR53
BASN313
BSER325

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 1512
ChainResidue
BTYR280
BARG283
CSER143
CASN195
CASN313
CHOH2103

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 1511
ChainResidue
ATYR280
AARG283
DTYR53
DASN195
DASN313

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1510
ChainResidue
AGLY54
AILE55
ATHR57
AGLN76
ALEU79
ALYS188
AGLU189
AGLY190
ALEU191

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL B 1510
ChainResidue
BGLY54
BILE55
BTHR57
BPHE59
BLEU72
BGLN76
BLEU79
BLYS188
BGLY190
BLEU191
BHOH2298

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL C 1510
ChainResidue
CILE55
CPHE59
CGLN76
CLEU79
CALA187
CLYS188
CGLY190
CLEU191
CHOH2050

site_idAC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL D 1510
ChainResidue
DGLY54
DILE55
DLEU72
DGLN76
DALA187
DLYS188
DGLU189
DGLY190
DLEU191
DHOH2290

Functional Information from PROSITE/UniProt
site_idPS00213
Number of Residues14
DetailsLIPOCALIN Lipocalin signature. GEGkaRYKGQWLSA
ChainResidueDetails
AGLY158-ALA171

site_idPS00488
Number of Residues17
DetailsPAL_HISTIDASE Phenylalanine and histidine ammonia-lyases signature. GSVGASGDLaPLAhmsL
ChainResidueDetails
AGLY138-LEU154

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: 2,3-didehydroalanine (Ser) => ECO:0000269|PubMed:7947813, ECO:0000269|PubMed:8204579
ChainResidueDetails
ASER143
BSER143
CSER143
DSER143

site_idSWS_FT_FI2
Number of Residues8
DetailsCROSSLNK: 5-imidazolinone (Ala-Gly)
ChainResidueDetails
AALA142
AGLY144
BALA142
BGLY144
CALA142
CGLY144
DALA142
DGLY144

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1b8f
ChainResidueDetails
AALA142
ATYR280
ASER143
AGLU414
AGLY144

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1b8f
ChainResidueDetails
BALA142
BTYR280
BSER143
BGLU414
BGLY144

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1b8f
ChainResidueDetails
CALA142
CTYR280
CSER143
CGLU414
CGLY144

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1b8f
ChainResidueDetails
DALA142
DTYR280
DSER143
DGLU414
DGLY144

site_idMCSA1
Number of Residues7
DetailsM-CSA 417
ChainResidueDetails
ATYR53electrostatic stabiliser
AHIS83electrostatic stabiliser
AASN195activator
ATYR280proton shuttle (general acid/base)
AARG283electrostatic stabiliser
AGLY329electrostatic stabiliser
AGLU414proton shuttle (general acid/base)

site_idMCSA2
Number of Residues7
DetailsM-CSA 417
ChainResidueDetails
BTYR53electrostatic stabiliser
BHIS83electrostatic stabiliser
BASN195activator
BTYR280proton shuttle (general acid/base)
BARG283electrostatic stabiliser
BGLY329electrostatic stabiliser
BGLU414proton shuttle (general acid/base)

site_idMCSA3
Number of Residues7
DetailsM-CSA 417
ChainResidueDetails
CTYR53electrostatic stabiliser
CHIS83electrostatic stabiliser
CASN195activator
CTYR280proton shuttle (general acid/base)
CARG283electrostatic stabiliser
CGLY329electrostatic stabiliser
CGLU414proton shuttle (general acid/base)

site_idMCSA4
Number of Residues7
DetailsM-CSA 417
ChainResidueDetails
DTYR53electrostatic stabiliser
DHIS83electrostatic stabiliser
DASN195activator
DTYR280proton shuttle (general acid/base)
DARG283electrostatic stabiliser
DGLY329electrostatic stabiliser
DGLU414proton shuttle (general acid/base)

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon