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3H5N

Crystal structure of E. coli MccB + ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004792molecular_functionthiosulfate-cyanide sulfurtransferase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0008641molecular_functionubiquitin-like modifier activating enzyme activity
A0016779molecular_functionnucleotidyltransferase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0004792molecular_functionthiosulfate-cyanide sulfurtransferase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0008641molecular_functionubiquitin-like modifier activating enzyme activity
B0016779molecular_functionnucleotidyltransferase activity
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0004792molecular_functionthiosulfate-cyanide sulfurtransferase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0008641molecular_functionubiquitin-like modifier activating enzyme activity
C0016779molecular_functionnucleotidyltransferase activity
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0004792molecular_functionthiosulfate-cyanide sulfurtransferase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0008641molecular_functionubiquitin-like modifier activating enzyme activity
D0016779molecular_functionnucleotidyltransferase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 500
ChainResidue
ACYS257
ACYS260
ACYS343
ACYS346

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
AATP502

site_idAC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ATP A 502
ChainResidue
AASP148
AASN154
AARG157
AGLN158
ALYS170
ALEU192
AASN193
AILE194
AALA213
AASP214
AHIS215
ALEU219
ATYR239
AHOH391
AHOH411
AMG501
AHOH513
AHOH574
BARG94
AGLY122
AGLY124
AGLY125
AASP146

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AASN59
AHOH682
AHOH722
BLYS278
BHOH609

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 500
ChainResidue
BCYS257
BCYS260
BCYS343
BCYS346

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 501
ChainResidue
BHOH362
BHOH385
BHOH396
BATP502

site_idAC7
Number of Residues32
DetailsBINDING SITE FOR RESIDUE ATP B 502
ChainResidue
AARG94
BGLY122
BGLY124
BGLY125
BASP146
BASP148
BASN154
BARG157
BGLN158
BLYS170
BLEU192
BASN193
BILE194
BALA213
BASP214
BHIS215
BLEU219
BTYR239
BHOH362
BHOH381
BHOH385
BHOH396
BHOH404
BHOH434
BHOH446
BHOH462
BHOH463
BHOH478
BMG501
BHOH510
BHOH526
BHOH648

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 500
ChainResidue
CCYS257
CCYS260
CCYS343
CCYS346

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG C 501
ChainResidue
CHOH367
CHOH378
CHOH391
CATP502

site_idBC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE ATP C 502
ChainResidue
CHOH368
CHOH378
CHOH391
CHOH414
CHOH465
CHOH476
CMG501
CHOH543
DARG94
CGLY122
CGLY124
CGLY125
CASP146
CASP148
CASN154
CARG157
CGLN158
CLYS170
CLEU192
CASN193
CILE194
CALA213
CASP214
CHIS215
CLEU219
CTYR239
CHOH367

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 500
ChainResidue
DCYS257
DCYS260
DCYS343
DCYS346

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG D 501
ChainResidue
DHOH373
DHOH389
DATP502

site_idBC4
Number of Residues29
DetailsBINDING SITE FOR RESIDUE ATP D 502
ChainResidue
DGLY122
DGLY124
DGLY125
DASP146
DASP148
DASN154
DARG157
DGLN158
DLYS170
DLEU192
DASN193
DILE194
DALA213
DASP214
DHIS215
DLEU219
DTYR239
DHOH360
DHOH373
DHOH389
DHOH411
DHOH461
DHOH468
DHOH473
DMG501
DHOH514
DHOH548
DHOH554
DHOH618

246905

PDB entries from 2025-12-31

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