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1MV5

Crystal structure of LmrA ATP-binding domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
B0005524molecular_functionATP binding
B0016887molecular_functionATP hydrolysis activity
C0005524molecular_functionATP binding
C0016887molecular_functionATP hydrolysis activity
D0005524molecular_functionATP binding
D0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG C 1601
ChainResidue
BADP1600
CASP2353

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG D 3601
ChainResidue
DSER3383
DADP3600
DHOH4046
DHOH4078

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ATP A 601
ChainResidue
AILE358
AGLY379
AGLY380
AGLY381
ALYS382
ASER383
ATHR384
AHOH4074
DSER3355
DGLU3356
DADP3600
ATYR352
AASP353
AGLU356

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ADP B 1600
ChainResidue
BTYR1352
BGLU1356
BILE1358
BSER1378
BGLY1379
BGLY1380
BGLY1381
BLYS1382
BSER1383
BTHR1384
CMG1601
CASP2353
CSER2355
CATP2601
CHOH4029

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ATP C 2601
ChainResidue
BASP1353
BSER1355
BGLU1356
BADP1600
CTYR2352
CSER2378
CGLY2379
CGLY2380
CGLY2381
CLYS2382
CSER2383
CTHR2384
CHOH4032

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ADP D 3600
ChainResidue
AASP353
ASER355
AATP601
DTYR3352
DGLU3356
DILE3358
DPRO3377
DSER3378
DGLY3379
DGLY3380
DGLY3381
DLYS3382
DSER3383
DTHR3384
DMG3601
DHOH4039

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. ISGGQRQRLAIARAF
ChainResidueDetails
AILE481-PHE495

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434
ChainResidueDetails
ALYS382
BLYS1382
CLYS2382
DLYS3382

218500

數據於2024-04-17公開中

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