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4G37

Structure of cross-linked firefly luciferase in second catalytic conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004467molecular_functionlong-chain fatty acid-CoA ligase activity
A0004497molecular_functionmonooxygenase activity
A0005524molecular_functionATP binding
A0005777cellular_componentperoxisome
A0008218biological_processbioluminescence
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
A0046949biological_processfatty-acyl-CoA biosynthetic process
A0047077molecular_functionPhotinus-luciferin 4-monooxygenase (ATP-hydrolyzing) activity
A0051087molecular_functionprotein-folding chaperone binding
B0000166molecular_functionnucleotide binding
B0004467molecular_functionlong-chain fatty acid-CoA ligase activity
B0004497molecular_functionmonooxygenase activity
B0005524molecular_functionATP binding
B0005777cellular_componentperoxisome
B0008218biological_processbioluminescence
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
B0046949biological_processfatty-acyl-CoA biosynthetic process
B0047077molecular_functionPhotinus-luciferin 4-monooxygenase (ATP-hydrolyzing) activity
B0051087molecular_functionprotein-folding chaperone binding
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE SLU A 601
ChainResidue
AHIS245
AGLY339
AGLY341
ALEU342
ATHR343
AALA348
AASP422
AARG437
ALYS439
ALYS443
AGLN448
APHE247
AHOH735
AHOH772
AHOH773
ATHR251
ASER314
AGLY315
AGLY316
AALA317
APRO318
AGLN338

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE XLX A 602
ChainResidue
ACYS108
ALYS445
ACYS447

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 603
ChainResidue
ATYR70
ALYS148
AGLN162
AHIS171

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 604
ChainResidue
ALYS380
AARG393

site_idAC5
Number of Residues22
DetailsBINDING SITE FOR RESIDUE SLU B 601
ChainResidue
BHIS245
BPHE247
BTHR251
BGLY315
BGLY316
BALA317
BPRO318
BGLN338
BGLY339
BTYR340
BGLY341
BLEU342
BTHR343
BALA348
BASP422
BLYS439
BLEU441
BLYS443
BGLN448
BHOH757
BHOH791
BHOH808

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE XLX B 602
ChainResidue
BCYS108
BLYS445
BCYS447

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 603
ChainResidue
BARG261
BHOH761

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 604
ChainResidue
BTYR70
BLYS148
BGLN162
BHIS171

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 605
ChainResidue
BARG393
BASP415
BTRP417

Functional Information from PROSITE/UniProt
site_idPS00455
Number of Residues12
DetailsAMP_BINDING Putative AMP-binding domain signature. IMNSSGSTGlPK
ChainResidueDetails
AILE195-LYS206

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 128
ChainResidueDetails
AARG218electrostatic stabiliser
AHIS245electrostatic stabiliser
ATHR343electrostatic stabiliser, hydrogen bond donor
ALYS443electrostatic stabiliser, hydrogen bond donor
ALYS529electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 128
ChainResidueDetails
BARG218electrostatic stabiliser
BHIS245electrostatic stabiliser
BTHR343electrostatic stabiliser, hydrogen bond donor
BLYS443electrostatic stabiliser, hydrogen bond donor
BLYS529electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-04-24

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