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1JJ7

Crystal Structure of the C-terminal ATPase domain of human TAP1

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 902
ChainResidue
AHOH36
AHOH40
AHOH46
AHOH61
ASER545
AADP752

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE ADP A 752
ChainResidue
AHOH19
AHOH33
AHOH36
AHOH40
AHOH46
AHOH62
AHOH82
AHOH103
ATYR512
AARG515
AVAL520
APRO539
AASN540
AGLY541
ASER542
AGLY543
ALYS544
ASER545
ATHR546
ATHR613
AVAL617
AMG902
AHOH4
AHOH7
AHOH13

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRQAVALARAL
ChainResidueDetails
ALEU643-LEU657

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P36370, ECO:0000255|PROSITE-ProRule:PRU00434
ChainResidueDetails
AGLY538

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:11532960, ECO:0007744|PDB:1JJ7
ChainResidueDetails
ASER545

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P36370
ChainResidueDetails
ASER641
AGLN701

226707

PDB entries from 2024-10-30

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